Learning activity 4.3_ Exploring protein synthesis

9/16/24, 12:34 PM Learning activity 4.
3: Exploring protein synthesis
 Learning Goals
How many different letters do you notice in the image above?
Those four letters above – A, C, G, and T – represent each of the different types of nucleic
acids that make up DNA, which is responsible for all the incredible diversity of life.
How is it that the “language” of DNA only has 4 letters, but we see such a huge amount of
diversity?
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9/16/24, 12:34 PM Learning activity 4.3: Exploring protein synthesis
You've already learned that proteins are formed by long chains of amino acids linked
together by peptide bonds and then folded together. DNA is made up of nucleic acids, of
which there are four types. DNA is like a recipe for amino acids. Each amino acid is specified
by a three nucleic acid “word” called a codon. Try the activity below to see how complex
messages can be represented with a simple system of four letters and three-letter words.
DNA coding
Use the guide below to decode the messages written in code using DNA codons.
Notebook
Decode the following messages in your notebook before checking the

suggested answers.
NOTE: Every time the codon TTG appears, that indicates a space in between two words.
CTC ACA AAG ATG AAT AGA ATC ACG TTG CTC GCT CGG TTG AGA CAG TTG ACC CCA
ATC
Hide Suggested Answer
Answer: Decoding DNA is fun.
2) GAC CCA ATA AAA ATC TTG CTC GCT CGG TTG AAG ATG ATC CAT AAA AGA ATC
CAG TTG TCG TTG AAC AGA AGT AGT AGA ATG ATC TTG AAC AAA CAG ACA TTG ATT
AAA AGA CAC CAG
Answer: Human DNA contains 3 billion base pairs.
3) GTC ACT ACA TTG CAT ATG CAT AAA AGT TTG AGT ACA ATC ACG CAT ACT TTG ATG
ACC TTG CTC GCT CGG TTG AGA ATC TTG TCA TTG ACT CCA ATA AAA ATC TTG ACA
CAA CCA AAA AGT CAG TTG TGG TTC TTG CAC ATG CCA ATC AAT TTG CAT CAC AGA
ATT CAG TTG ACC CAC ATG ATA TTG CAT ACT ACA TTG CTG AAA CAC CAT ACT TTG
CAT ATG TTG CAT ACT ACA TTG GTA CCA ATC
Answer: The total length of DNA in one human equals 70 round trips from the
earth to the sun.
The importance of protein synthesis

The information stored in genes can only be useful to a cell if it is read and turned into
proteins. DNA is like an architect’s plan for a house; it tells the builders how to construct it.
But the genes themselves cannot assemble a protein on their own any more than an
architect’s drawing can pick up a hammer and start building a house. Both genes and
architectural drawings need builders to turn their plans into reality. Within cells, there is an
extensive set of biochemicals that builds proteins, based on the instructions read from the
DNA. This process is called protein synthesis.
Not all the genes in a cell are synthesized into proteins. Another way to say this is that the
genes are not “expressed.” For example, the cone cells in your eye have the same set of
genetic instructions as the insulin-producing cells in your pancreas, but your eye can’t
manage blood glucose levels any more than your pancreas can help you to see. So how do
the cone cells know that they should do only one job, when their DNA contains the
information for doing every job? The answer lies in gene expression. Somehow, just the
right genes are read at just the right time to make the proteins needed for that cell, at that
moment. The way that genes are expressed depends on a complex interaction between the
genetic code and environmental conditions.
Biologists are discovering the importance of understanding gene expression. When genes
are being expressed and are creating proteins, geneticists say they are “turned on,” and
when they are not, they are “turned off.”
Understanding what causes genes to turn on and off has the potential to explain how we
develop and age, as well as explaining the origins of many important diseases like cancer
and heart disease.
Explore this!
To learn more, you may choose to explore this optional video from
Cancerquest on how genes turn on and off
(https://www.youtube.com/watch?v=46Xh7OFkkCE), and how that
connects to cancer or perform your own research on the topic.
The excitement over the potential medical breakthroughs offered by understanding gene
expression has biologists intensively studying all aspects of the protein synthesis process,
particularly the roles of RNA. In 2010, University of Toronto researchers announced that they
had cracked the “second genetic code,” which lets them predict how a gene will be
expressed under different conditions. Their discovery solves a mystery that had been around
since the human genome was sequenced and found to contain only 20,000 genes. Other
simpler species, like trees, can have three times that amount. How can humans create
organs as complex as brains, using so few genes? The answer is that each gene can be
expressed in many ways, depending on what happens to the RNA.
Before you learn the technical details of protein synthesis, it helps to first get an overview of
the whole process and to learn about some of the discoveries that got us to this point.
Understanding checkpoint: The importance of protein synthesis
Question 1 of 1
How can each cell in the human body perform its own specialized function, if all
cells have the same genetic information?
Not all genes in a cell are expressed and turned into proteins.
Only those genes related to the cell’s specialized function are expressed.
Each cell uses a subset of the total genetic code to meet its specialized needs.
All of the above.
Submit
 You are correct. All of the statements answer the question.

Your score is 1 out of 1.
Overview of the protein synthesis process

Recall that proteins are made of polypeptides, which are long chains of amino acids joined
together by peptide bonds. The sequence of amino acids determines the protein’s final
shape and function. The sequence of amino acids for a protein is coded in the DNA. Protein
synthesis is the process by which the genetic code in the DNA is decoded through different
kinds of RNA into amino acids and eventually, proteins.
The two main stages in Protein Synthesis are:

Transcription
In eukaryotes the process starts in the nucleus and ends in the cytoplasm. The
section of DNA where the gene is being expressed is unwound, in order to give
messenger RNA (mRNA) access to transcribe (copy) it. This is called the
transcription stage.

Translation
The mRNA containing the genetic information then leaves the nucleus, while the
DNA stays safely behind. The mRNA enters the cytoplasm, where it attaches to
ribosomes. Ribosomes travel along the mRNA strand, providing a site where transfer
RNA (tRNA) can translate the mRNA’s genetic code into a polypeptide chain, one
amino acid at a time. This is called the translation stage.
When done, the polypeptide chain is released and it quickly folds up into a complex
shape determined by its amino acid sequence. This shape is the final protein. The
ribosomes mRNA and tRNA are then reused by the cell to make other proteins.
Overview of the process of protein synthesis in eukaryotes. DNA is transcribed into

mRNA, which travels to the cytoplasm where it translates the genetic code into a
polypeptide that ultimately folds into the protein.
The “central dogma” of genetics

The process of protein synthesis follows a one-way sequence from DNA to protein (Figure
below). This process is not reversible. Changes in DNA can result in changes in the protein,
but changes in the protein will not change the DNA.
Caption: Overview of the protein synthesis process: DNA undergoes transcription to make
RNA. Then, RNA undergoes translation to make protein. Note: that the arrows only go in
one direction.
The overall process summarized in the image was proposed by Francis Crick, the co-
discoverer of the structure of DNA. He called this two-step process the “central dogma” of
genetics. By this he meant that it was a powerful theory, but at the time had little
experimental support. That experimental evidence has since been found, proving Crick right.
Early research into protein synthesis

When Gregor Mendel published his work on the inheritance of physical traits in pea plants,
he showed that discrete genes were responsible for discrete phenotypic characteristics. This
was the first time that anyone had demonstrated a relationship between genotype and
phenotype. The next step would be to find the type of molecules that were determined by
the genes.
That step was reached in the early 1900s when a British doctor, Archibald Garrod,
hypothesized that protein was the type of molecule determined by the genes. He noticed that
certain illnesses were more common in some families than others, indicating that the
illnesses were inherited. Garrod studied patients suffering from a rare genetic disease that
caused their urine to turn black when exposed to air. He identified a mutation in a gene
coding for the enzyme (protein) involved in the metabolism of urine production.
He showed that these patients were unable to produce the correct form of the enzyme
because the gene responsible for it was faulty.
One gene-one polypeptide hypothesis

Garrod’s work showed that genes somehow coded for proteins, but exactly how this
happened remained a mystery for the next 40 years. The work of American researchers
George Beadle and Edward Tatum in the 1940s revealed the one-to-one relationship
between genes and proteins.
Beadle and Tatum studied how different genetic strains of a bread mould synthesized an
amino acid, arginine. Four enzymes are needed to fully synthesize arginine along a
biochemical pathway. They isolated four mutant strains of the moulds and showed that each
one lacked the ability to make one of the four enzymes. They also showed that each strain
had a mutation in a different gene, and that each mutation only affected one enzyme. The
pattern they detected of one gene affecting only one enzyme is now called the one gene-one
polypeptide hypothesis.
Since then, research has shown that in some cases, one gene can code for more than one
polypeptide. You will learn more about this in later sections.
How mutations cause disease

How a mutation in one gene can be responsible for a human disease was first shown in 1956
by Vernon Ingram. Ingram compared the amino acid sequences of the protein hemoglobin
(the molecule that carries oxygen in red blood cells) in people with healthy red blood cells to
those with a genetic disease called sickle-cell anemia.
Ingram used the technique of electrophoresis to determine the amino acid sequence of the
polypeptides that make up the protein. He found that the patients with sickle-cell anemia
differed from the healthy patients in only one amino acid on one polypeptide chain in
hemoglobin. In healthy patients, the amino acid glutamate is present at a certain location on
the β-hemoglobin polypeptide, but in patients with sickle-cell anemia, that location contains
the amino acid, valine, instead.
This one change in the amino acid sequence changes the way in which the resulting
polypeptide coils up. This affects its shape and ultimately affects the way that the hemoglobin
protein functions. This was the first time that a researcher had demonstrated that a single
amino acid exchange in a protein can cause a disease or disorder.
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Discovering the genetic code

To early researchers, the DNA sequence was a mysterious string of nucleotide bases, like
letters of the alphabet in a foreign language. They knew that sections of the sequence must
code for individual proteins and that within those sections, groups of letters must code for
individual amino acids, but they did not know how this was done. They had found the
alphabet but couldn’t recognize the words. The challenge now was to crack the genetic code
and find the words among the letters.
Francis Crick proposed that three sequential nucleotide letters (for example, ACG) made up
a unit that coded for a particular amino acid. He called these units codons. Crick’s proposal
was called the triplet hypothesis. He based his hypothesis on the fact that DNA contained
four different letters and there were 20 different amino acids.
If only one nucleotide were used to code for an amino acid, then DNA could only code
for four different amino acids.
If two nucleotides combined to form a codon, then that would give 4 × 4 =16 different
combinations, but again, not enough to code for all 20 amino acids.
However, if three nucleotides together formed a codon, then they would be able to
code for 4 × 4 × 4 = 64 different amino acids. This was more than enough. Crick tested
his hypothesis in experiments on bacteria and, in 1961, he was able to confirm that the
triplet hypothesis was correct.
Later the same year, two other researchers, Marshall Nirenberg and Har Gobind Khorana,
were able to identify the triplet letter sequences (codons) that coded for each of the 20 amino
acids. For their work in discovering the genetic code, they received the Nobel Prize in
Physiology/Medicine in 1968.
The table below shows the codons used to code for each amino acid. (Note: You do not
have to memorize the contents of this table for this course). Because amino acids are
actually coded for using RNA instead of DNA, there is one change in the base pairs used in
the coding. The nucleotide thymine (T) in DNA is replaced with uracil (U) in RNA.
Because there are 64 potentially different codons and only 20 different amino acids, there is
some redundancy in the codes. Most amino acids can be coded by more than one codon.
This redundancy helps to reduce the impact of minor mutations, since not all mutations will
result in changes in the amino acid sequence. Only three codons do not code for any amino
acid. These codons (UAA, UAG, and UGA) are used to make protein synthesis stop. One
codon, AUG, is used to indicate the start of the protein synthesis sequence, as well as coding
for methionine.
Second letter
First letter U C A G Third letter
U Phenylalanine Serine Tyrosine Cysteine U
Phenylalanine Serine Tyrosine Cysteine C
Leucine Serine STOP STOP A
Leucine Serine STOP Tryptophan G
C Leucine Proline Histidine Arginine U
Leucine Proline Histidine Arginine C
Leucine Proline Glutamine Arginine A
Leucine Proline Glutamine Arginine G
A Isoleucine Threonine Asparagine Serine U
Isoleucine Threonine Asparagine Serine C
Isoleucine Threonine Lysine Arginine A
START/Methionine Threonine Lysine Arginine G
G Valine Alanine Aspartate Glycine U
Valine Alanine Aspartate Glycine C
Valine Alanine Glutamate Glycine A
Valine Alanine Glutamate Glycine G
In the table above, each three-letter codon is read from left to right across the columns of the
table, indicating their positions within the codon. For example, the codon CAU codes for
histidine, CAA codes for glutamine, and UGG codes for tryptophan.
At first, it was thought that this genetic code was universal—that all organisms used the
same codons to code for the same amino acids. A few exceptions have been found in the
genetic codes in mitochondria and chloroplasts but, generally speaking, this genetic code is
the same in all organisms.
Try It!
Write a codon for Lysine.
Codon 1: AAA or Codon 2: AAG
Understanding checkpoint: The genetic code
Question 1 of 1
Where is the DNA during the transcription process in eukaryotic cells?
cytoplasm
nucleus
matrix
mitochondria
Submit
 Yes, this is correct. Transcription occurs in the nucleus.

Solve this hypothetical amino acid sequence by translating the mRNA codons into amino
acids, using the genetic code in the table above. Recall that T in DNA is replaced with U in
RNA, which is why an A in the DNA codon is complemented by a U, instead of a T, in the
mRNA codon.
DNA codon (5 - TAC TAG AAA TCT GCG ATG ATT

3)
mRNA codon AUG AUC UUU AGA CGC UAC UAA
Amino Acid Methionine (also Iso- Pheny- Argi- Argi- Tyro- STOP
START) leucine lalanine nine nine sine
Show Answers
Question 1 of 1
The figure below represents the ‘central dogma’ of genetics. True or false?
true
false
Submit
 Yes, this is exactly what the ‘central dogma’ of genetics states.

In a sentence, explain the one gene-one polypeptide hypothesis and describe one example
of evidence that supports the hypothesis.
The one One example is the studies done by researchers Beadle and
gene-one Tatum, who studied how different genetic strains of a bread
polypeptide mould synthesized an amino acid, arginine. Four enzymes
hypothesis are needed to fully synthesize arginine along a biochemical
says that pathway. They isolated four mutant strains of the moulds and
one gene is showed that each one lacked the ability to make one of the
responsible four enzymes. They also showed that each strain had a
for mutation in a different gene, and that each mutation only
producing affected one enzyme. The pattern they detected of one gene
one affecting only one enzyme is now called the one gene-one
polypeptide. polypeptide hypothesis. Vernon Ingram was the researcher
who discovered that the disease known as sickle-cell anemia
was the product of individual faulty genes coding for
individual amino acids that make up one of the β-hemoglobin

polypeptides. Each mutation in a gene corresponded to a
change in only one amino acid.
Explain why a codon that is two nucleotides long would be unable to code for all 20 amino
acids.
Because there are only four nucleotide bases, a codon that is two nucleotides
long could only code for a maximum of 4 × 4 = 16 amino acids. This is less than
the 20 needed.
Exploration
Using the interactive activity: Gene Expression PhET
(https://phet.colorado.edu/sims/html/gene-expression-essentials/latest/gene-
expression-essentials_en.html)
Before exploration:
Ask yourself the following questions to get your brain moving. Make rough notes on your
thoughts in your notebook.
1. What are genes?
2. Summarize transcription and translation.
3. What type of RNA have you already learned about?
Start (../ilo/gene_expression_essentials_phet/index.html?ou=23281821)

Exploration: Part 1
1. Enter by clicking on the “Expression” tab
2. Take a look at Gene 1. What type of macromolecule do you think it is (protein,

carbohydrate, nucleic acid, lipid)?
Show Suggested Answer
There are two regions of gene 1. What are they and what do you think the purpose
of each region is, based on their names?
1. Drag the RNA Polymerase from the tool box and place it on the dotted spot on
the gene. Record your observations.
2. Drag the negative transcription factor to the regulatory region of gene 1 and
drag the RNA polymerase again to the gene. Record your observations.
3. Consider what the purpose of the regulatory region of the gene is. Record your
thoughts.
4. Drag the RNA polymerase back to the tool box.
5. Drag the positive transcription factor from the tool box and fit it in its
appropriate location in the gene. Afterwards, take the RNA polymerase again
and fit it into the dotted spot.
6. Repeat dragging the RNA polymerase to its location on gene 1 while the
positive transcription factor is still attached to the regulatory region.
7. Record your observations
8. Make notes on the purpose/roles of the regulatory region, positive transcription

factor and RNA polymerase in the process of transcription
9. Take the positive transcription factor and RNA polymerase back to the tool box.
10. Take the ribosome from the tool box to the mRNA molecule.
11. Take the mRNA destroyer to the mRNA. Record your observations.
12. Brainstorm and make notes - what is the purpose and role of the mRNA
destroyer? What would happen if there was no mRNA destroyer?

Exploration: Part 2
1. Click “Next Gene” to move to gene 2
2. What is the difference that you notice in the tool box?
3. Brainstorm or predict what you think the second positive transcription factor
might do. What might be the advantages and disadvantages of having two
positive transcription factors? Record your ideas.
4. Move the first positive transcription factor to the gene.
5. Move the RNA polymerase to the gene.
6. Observe and record your results.
7. Drag the second positive transcription factor to the gene.
8. Again, move the RNA polymerase to the gene.
9. Observe and record the results.
After exploration: Part 2
Consider the following questions and then compare your answers to the suggested
answers.
1. Why is it important to destroy the mRNA after making a sufficient amount of

protein?
2. How will positive and negative transcription factors help maintain the homeostasis
of the body system?
3. Give an example of where gene expression without regulation could potentially

harm the organism.

Exploration: Part 3
1. Click on the box that says mRNA (along the bottom). You are given a gene with
the same regulatory and transcribed regions. You should explore the different
settings and factors. What things can you do with these factors to make the
rate of transcription the fastest possible? Make notes on your observations.
2. What are the three factors that impact the rate of transcription? Make note of
these three factors.
3. Select the “negative transcription factor” checkbox. What happens when you
increase the concentration and affinity of the negative transcription factor? And
if you also decrease the concentration and affinity of the positive factor to low?
Make notes on your observations.
Protein synthesis
In eukaryotes, protein synthesis happens in two main stages, with three phases in each.
The first main stage, transcription, happens within the nucleus. This is where the
genetic code stored in the DNA gets transcribed into an RNA copy of the information.
The second main stage, translation, happens in the cytoplasm. This is where the
genetic information in the RNA gets translated into a sequence of amino acids and
eventually, a protein.
This flow-chart represents the overall pathway for protein synthesis:
DNA → mRNA → Protein
You may be asking yourself why the eukaryotic cell bothers with this two-stage process.
Wouldn’t it be easier if the DNA were directly translated into proteins in the cytoplasm,
instead of using RNA as an intermediate step? The answer is no, for many reasons. A main
reason is that the cytoplasm is a very dangerous place for DNA molecules. There are lots of
enzymes and chemicals floating around that could permanently damage the DNA molecules
and so destroy the recipe needed to keep the cell alive. That is why eukaryotic DNA is kept
safely stored in the nucleus, protected by the nuclear membrane. RNA works like a
temporary and throw-away copy of the DNA.
The stages of protein synthesis can be summarized as follows:
The two stages of protein synthesis: DNA → mRNA → Protein
Stage 1 Stage 2
Stage 1: Transcription - Making an RNA copy of the gene
DNA→ mRNA → Protein
Occurs in the nucleus:
Phase 1: Initiation of mRNA transcription
Phase 2: Elongation of mRNA
Phase 3: Termination of mRNA transcription
Stage 2: Translation - Reading the RNA copy and assembling the

polypeptide
Occurs in the Cytoplasm
Phase 1: Initiation
Phase 2: Elongation (making the polypeptide)
Phase 3: Termination
You will learn the details of each stage and phase in the following sections. The process of
protein synthesis in prokaryotes is slightly different from that in eukaryotes, because
prokaryotes do not have a nuclear membrane and their DNA is arranged slightly differently.
The descriptions that follow apply to eukaryotes, unless stated otherwise.
The process is quite complex, so a lot has been left out in this learning activity to make it as
simple and clear as possible. If you would like to explore protein synthesis in more detail,
there are many great resources available on the internet, including animations of each stage.
You can search for these using terms like “protein synthesis,” “DNA transcription,” and “DNA
translation.”
To learn more, you may choose to watch one of the following videos to get an overview of
protein synthesis, read the article or perform your own research.
Explore this!
Please explore one of the following videos (or both if you would like to):
Choice 1 - Protein synthesis: The amoeba sisters

(https://youtu.be/oefAI2x2CQM)
Choice 2 - Protein synthesis: Fuse school

(https://www.youtube.com/watch?v=x5ZXQo-xeMo)

Stage 1: Transcription

In this stage a messenger RNA (mRNA) molecule is transcribed (copied) from the
DNA template by RNA polymerase. The objective is to make an accurate RNA copy
of the gene. This requires a three-phase process:
1. Initiation of mRNA Transcription
2. Elongation of mRNA
3. Termination of mRNA Transcription

Phase 1: Initiation
Template strand
DNA is made of two complementary strands of nucleotides twisted into a

double helix, but only one of them is used for protein synthesis. The strand
used for protein synthesis is called the template strand (sometimes also
called the sense strand). The other strand, known as the untranscribed
strand (also called the anti-sense or coding strand), does not code for
proteins.
RNA polymerase
To make the mRNA, the two DNA strands must be separated and the
template strand has to be transcribed in the correct direction, starting at the
correct nucleotide. An enzyme called RNA polymerase separates the two
DNA strands and then binds onto the template strand at the starting point, for
the gene to be read.
Promoter sequence
The RNA polymerase attaches at a point along the DNA called a promoter
sequence. This is located several nucleotides up from where the
transcription begins (by convention, the promoter sequence is usually shown
for the untranscribed strand). The DNA nucleotides in this region are mostly
thymine (T) and adenine (A), so this region is often called a TATA box. The
presence of the promoter sequence ensures that the RNA polymerase
begins transcribing at the right place, at the very start of the gene.
The initiation process is similar in both eukaryotes and prokaryotes, although

prokaryotes require a longer promoter sequence to get the RNA polymerase
to attach.

Phase 2: Elongation
Making messenger RNA (mRNA) and transcription

bubbles
Unlike in DNA replication, the RNA polymerase does not need a primer to
start adding nucleotides.
Once the RNA polymerase has bonded to the DNA molecule, it

unwinds the double helix and separates about 17 base pairs of DNA at
a time.
RNA polymerase unravels the coiled DNA as it moves along, forming a
transcription bubble behind it. Only the small segment of DNA being
actively transcribed by the RNA polymerase is exposed during
transcription.
Free-floating RNA nucleotides are added to the 3’ end of the growing
mRNA strand as the RNA polymerase moves down the DNA template
strand in the 3’ to 5’ direction.
When adenine (A) is encountered in the DNA, RNA polymerase adds
the nucleotide uracil (U), instead of thymine (T), to the growing mRNA
strand.
Just like in DNA replication, phosphodiester bonds between the 5’
phosphate and 3’ OH group of the previous nucleotide are formed to
join the mRNA nucleotides together.
The two DNA strands quickly rejoin and rewind into their double-helix
form once the polymerase has moved on. This is essential because
harmful enzymes (endonucleases) floating inside the nucleus would
destroy any exposed DNA.
When the bubble closes up, another RNA polymerase enzyme can
attach and start transcribing the same gene again. In this way, many
thousands of mRNA molecules can be transcribed from the same gene
in a short amount of time.

The final stage of transcription is devised of two important stages that

involve the termination of mRNA transcription and the modification of the
mRNA transcript before it leaves the nucleus. The two stages are:
1. Termination sequence: GC hairpin
2. Post-transcriptional Modifications in Eukaryotes
Termination sequence: GC hairpin
RNA polymerase continues to add RNA nucleotides to the growing mRNA

strand until it reaches a sequence of DNA nucleotides that tells it to stop.
This termination sequence is found at the end of the gene. The termination
sequence is actually a loop of guanine-cytosine pairs called a GC hairpin,
which acts like a bump in the road, to stop and dislodge the RNA
polymerase.
Once the process is terminated, the mRNA strand separates from the RNA
polymerase and travels to the cytoplasm for the next stage in making
proteins. The RNA polymerase separates from the DNA strand and is ready
to be reused again.
Post-transcriptional modifications in eukaryotes
In eukaryotes, the mRNA must be modified in two ways before it leaves the nucleus
to start making polypeptides in the cytoplasm.
Protecting mRNA against enzymes

Removing non-coding DNA called Introns
Protecting mRNA against enzymes
The first modification involves protecting the mRNA against enzymes. The cytoplasm
is rich with nucleases and phosphatases, enzymes that can break apart any
unprotected RNA or DNA strands. The presence of these enzymes in the same area
where protein synthesis occurs may seem counterproductive, but cells have evolved
these enzymes to protect themselves from infection by viral DNA and RNA.
Protection against the enzymes is done by placing extra nucleotide sequences on

both ends of the mRNA molecule. This is done using other enzymes which add:
a protective cap (guanine triphosphate (GTP)) at the 5’ end

a long series of repeating adenine nucleotides, called a poly-A tail, at the 3’

end.
The extra nucleotide sequence on both ends of the mRNA molecule:
protects the mRNA from damage in the cytoplasm.

helps the ribosomes determine which end they should bind to, for initiating
translation.
Removing non-coding DNA called introns
The second modification involves the code itself.
Eukaryotic genes include regions of non-coding DNA called introns, which are
stretches of DNA that do not get translated into proteins.
Introns separate coding regions called exons, which do get translated into proteins.
Since introns and extrons are both transcribed into the original mRNA molecule, the
introns must be removed before translation can occur.
Removal of the introns occurs using particles made of RNA combined with a protein
called spliceosomes. Spliceosomes cut out the introns and join up the remaining
exons to form a continuous coding sequence on the mRNA.
The following figure summarizes the sequence of the two post-transcriptional

modifications in eukaryotes.
The resulting mRNA is now called the mRNA transcript, which is ready to be sent
out to the cytoplasm for the translation stage in protein synthesis. This system may
seem unusual, but it turns out that these exons can be rearranged and joined
together in different arrangements with the result that the approximately 20,000
genes in humans can produce around 120,000 different proteins! Understanding how
RNA is modified after transcription promises to be one of the biggest discoveries in
genetics since the discovery of DNA.
In prokaryotes, the final process is a bit different. They lack a nucleus so their DNA is
always in the cytoplasm, where ribosomes can actually bind to the growing mRNA
strand and begin translation before RNA polymerase has even finished transcribing
the entire mRNA strand.
Understanding checkpoint: Protein synthesis – transcription
1) Place the following translation steps of in the correct sequence as they occur in
protein sequence. Press submit when you are ready to check your answers.
RNA polymerase unravels the coiled DNA as it moves

select:
along, forming a transcription bubble behind it
Protection against the enzymes is done by placing extra

select:
nucleotide sequences on both ends of the mRNA molecule
The RNA polymerase attaches at a point along the DNA

select:
called a promoter sequence.
The mRNA transcript, which is ready to be sent out to the

select:
cytoplasm for the translation stage in protein synthesis
RNA polymerase continues to add RNA nucleotides to the

select:
growing mRNA strand until it reaches a sequence of DNA
nucleotides that tells it to stop.
Removal of the introns occurs using particles made of RNA

select:
combined with a protein called spliceosomes.
Free-floating RNA nucleotides are added to the 3’ end of

select:
the growing mRNA strand as the RNA polymerase moves
down the DNA template strand in the 3’ to 5’ direction.
An enzyme called RNA polymerase separates the two DNA

select:
strands and then binds onto the template strand at the
starting point, for the gene to be read.
Submit
2) Transcribe the DNA codons shown below into the corresponding codons of their
mRNA strands.
CCT
select:
GAT
select:
AGA
select:
TCT
select:
GAG
select:
ACT
select:
TAT
select:
Submit
3) A geneticist decided to insert a gene for human growth hormone into bacteria to
create a way to produce large amounts of the hormone for medical use, but the
protein produced by the bacteria was not the same as the one produced in humans.
Explain why this may have happened.

Stage 2: Translation

In this stage, the mRNA transcript is translated into chains of amino acids by
ribosomes in the cytoplasm. Ribosomes are the “factory” where individual amino
acids are assembled into proteins. The amino acids are brought to the ribosomes by
transfer RNAs (tRNA).
This is called the translation stage because this is where the genetic code in the
DNA gets translated into proteins.
As with transcription, the process of translation also follows a three-phase process

of:
1. Initiation
2. Elongation
3. Termination
Phase 1: Initiation
The modified mRNA transcript enters the cytoplasm where a ribosome attaches to it.
Ribosomes are complexes of proteins and RNA (called ribosomal RNA or rRNA),
arranged into two parts called the large and small subunits. The ribosome is the
structure on which amino acids get joined together to form the desired polypeptide
chain.
The whole initiation process is quite complex, but can be broken down into three
steps:
Step 1: Ribosome begins attachment to mRNA

Step 2: Initiator tRNA-amino acid pair Is created in cytoplasm
Step 3: Initiator tRNA-amino acid pair attaches to the ribosome
Let’s take a closer look at each of the steps.

Step 1: Ribosome begins attachment to mRNA
At the beginning of initiation:
the small subunit of the ribosome attaches to the mRNA strand near
the start codon, AUG, which codes for the amino acid methionine.
the large subunit joins in later, to help sandwich the mRNA transcript
between the two subunits.
some proteins, called initiation factors, also combine with the two
ribosome subunits. Together they form an initiation complex that
stabilizes the mRNA and helps to ensure that the ribosome is
positioned correctly on the mRNA to begin reading the code.
The initiation process in prokaryotes is a bit different, as they have fewer

initiation factors and form a less complicated initiation complex.

Step 2: Initiator tRNA-amino acid pair Is created in cytoplasm
In the cytoplasm, free-floating tRNA gets attached to an amino acid using the
enzyme aminoacyl-tRNA synthetase to form a temporary complex called
aa-tRNA complex (where aa stands for the particular amino acid used).
Each tRNA is built to normally bond with only one kind of amino acid (in
some cases, a few kinds). A tRNA carrying an amino acid is said to be a
“charged” tRNA.
One kind of tRNA, called tRNAmet, joins with the amino acid methionine
(met). This creates a temporary amino acid complex called the met-tRNAmet
complex. This complex is called the initiator tRNA and is used to position
the first amino acid in the polypeptide chain.
Step 3: Initiator tRNA-amino acid pair attaches to the


ribosome
The met-tRNAmet complex (initiator) attaches to the ribosome at the AUG

“start” codon. It does this because the three-nucleotide sequence (UAC) at
the bottom of the tRNA molecule is the complement (or anti-codon) to the
AUG codon on the mRNA.
Each active ribosome has four binding sites: one for the mRNA transcript,
and three sites (E, P, and A) for binding tRNA molecules. The met-tRNAmet
attaches to the P site above the start codon on the mRNA.
Once the ribosome is fully set up on the mRNA transcript, the synthesis of
the polypeptide can begin.
Phase 2: Elongation
The procedure of attaching amino acids together into a polypeptide chain involves a
cycle with four steps:
1. New amino acid is brought to the A site by its charged aa-tRNA complex
2. New amino acid is bonded to the growing polypeptide chain
3. Ribosome moves forward one codon; all aa-tRNAs move one site backwards
4. The A site is available to receive another charged aa-tRNA complex and the
uncharged tRNA on the E site is released to be reused

Step 1
The amino acid that corresponds to the codon positioned under the A
(“acceptor”) site is brought in to the A site by its aa-tRNA complex. The
matching of the tRNA anti-codons to the mRNA codon ensures that the
correct amino acids are being added in the correct sequence. The aa-tRNA
complex attaches to the A site by forming a weak hydrogen bond with the
mRNA.

Step 2
The two amino acids are placed close enough to one another for a peptide
link to form between them. Enzymes in the large subunit catalyze the
formation of the peptide bond between the amino acid sitting in the P site
and the new amino acid at the A site.

Step 3
The ribosome moves forward one codon towards the 3’ end. As a result, the
aa-tRNA on the A site becomes translocated to the P site (“peptidyl”) of the
ribosome. This frees up the A site to accept a new amino acid. The tRNA that
was on the P site is now uncharged and it moves to the E (“exit”) site.

Step 4
The cycle repeats. The ribosome again moves forward one codon, the
tRNAs get translocated one site backward, and the uncharged tRNA on the
E site gets released to the cytoplasm to be reused.
This elongation cycle continues until the ribosome reaches the end of the
mRNA transcript. Some proteins contain a few hundred amino acids, while
others, like some muscle proteins, can be 27,000 amino acids in length.
Elongation continues until a stop or termination codon is encountered on the mRNA

transcript. In the following image you can see that there are three “stop” codons
(UAA, UAG, and UGA). A special protein release factor recognizes these stop
codons and triggers the termination of translation.
When the termination codon is reached, the two ribosome subunits and associated
initiation complex proteins break off from the mRNA strand. The completed
polypeptide is then folded into its final conformation by other proteins to produce its
functional form.
Understanding checkpoint: Translation
Read the following statements about protein synthesis and determine if they are true
or false.
Question 1 of 4
The role of rRNA is to provide a temporary copy of the gene in the DNA
blueprint and attach that copy to the ribosome, where the correct sequence
of amino acids can be joined together.
True
False
Submit Next 
The regulation of protein synthesis

Every living cell can respond to its environment by changing the types and amounts of
protein it produces through changes in its gene expression. For example, some proteins are
only necessary during key moments in a cell’s life cycle, while others may be needed
constantly. As you have probably recognized, the process of protein synthesis is
energetically costly for organisms. Anabolic (building) processes require energy. Because of
the high cost of making proteins, they are only made when necessary. So, how does a cell
know to produce a protein only when needed? How does the cell start or stop the processes
of protein synthesis?
Regulation of protein synthesis occurs at four different levels of control:
1. Transcriptional
2. Post-transcriptional
3. Translational
4. Post-translational levels.
The following section will describe the four levels of control in more detail.
Transcriptional level
This regulation method determines which genes get transcribed or controls the rate at which
transcription occurs.
div class="row ilc-row-callout">

Explore this!
Explore the following video for an overview of gene regulation or perform your own
research on the topic.
Transcription factors
Transcription begins when RNA polymerase binds to the DNA at the promoter region. To help
RNA polymerase bind to the DNA, regulator proteins called transcription factors need to
bind onto the promoter region first. The presence and concentration of these transcription
factors determine whether a gene is transcribed and how fast transcription can occur. This
regulatory method is found in eukaryotes.
Operons
An operon is a group of genes under the control of a single regulatory protein. The result is
that the genes contained in the operon are either expressed together or not at all. In the
same way that you can use a power bar to turn many plugs on and off with one switch, one
operon can turn many genes on and off using one regulatory protein.
Operons are useful when all the genes in the operon are used to create proteins required in
the same biochemical pathway. Operons occur primarily in prokaryotes, but they have
recently been found in some eukaryotes.
The first operon discovered was in the bacteria, E. coli. The lactose (or lac) operon contains
two regions: control and coding.
The control region is made up of sequences of DNA called a promoter (Plac) and an
operator (O). Together, these determine whether the genes in the operon get
expressed.
The coding region contains the genes that code for the three enzymes (beta-
galactosidase, permease, and transacetylase) that work together to break down
lactose. Unless RNA polymerase can attach to the control region, it will be unable to
transcribe the genes for making the enzymes in the coding region.
The lac operon
Promoter
CAP site Operator lac Z lac Y lac A

Promotes blocks RNA
RNA + - polymerase
polymerase
binding Repressor
CAP
RNA Polymerase
Operons can operate using negative or positive regulation.
Negative regulation involves the binding of a regulatory protein (“repressor”) to the

operator to prevent transcription.
Positive regulation involves the binding of a regulatory protein (“activator”) to an area
close to the promoter region to stimulate transcription. The lac operon shows both
types of regulation.
Example of negative regulation
Negative regulation
No
Repressor transcription
Promoter Operator
Transcription
Promoter Operator
(No repressor)
To save energy, E. coli will not produce the lactase enzymes unless the sugar, lactose, is
present in the cells’ environment.
In the absence of lactose, a repressor protein (lacl) attaches to the operator region,
preventing the binding of RNA polymerase to the DNA strand.
When lactose is present, the repressor protein lacl releases itself, allowing RNA
polymerase to bind and turn on the lac operon.
This is an example of negative regulation because the attachment of the regulatory protein
turns the lac operon off.
Example of positive regulation
The lac operon also exhibits positive regulation to ensure that enough lactase is produced
when the cell needs it most. Recall that cells need glucose as a source of energy and that
glucose is a monosaccharide, while lactose is a disaccharide.
If enough glucose is available, the cell doesn’t need to waste energy breaking down a
disaccharide
But if glucose levels are low, then the cell needs the lactase enzymes to break lactose
down into glucose. When glucose levels are low, an activator protein will bind to a site
close to the plac promoter region. This makes it easier for the RNA polymerase to bind
to the promoter so that the lac genes will be transcribed at a higher rate.
Positive regulation
Activator Transcription
Promoter Operator
No
transcription
Promoter Operator
(No activator)
Post-transcriptional level
In eukaryotes, the mRNA molecule formed in the nucleus must be modified before it can
become the mRNA transcript in the cytoplasm. If the 3’ poly-A tail and 5’ cap are not added,
translation can be blocked in two simple ways:
If it lacks the poly-A tail, then the mRNA strand will not be able to leave the nucleus.
If it also lacks a cap, nucleases (enzymes) will break it up, back into its individual
nucleotides.
Translational level
Regulatory proteins in the cytoplasm can bind near the 5’ cap of an mRNA transcript. The
small ribosomal subunit is then unable to attach to the mRNA transcript, because the
proteins have covered the first few nucleotides where it would normally attach. These
proteins can be removed to allow translation to restart.
Post-translational level
Once the polypeptide is released from the ribosome, it can be modified by chaperone
proteins. These proteins affect the way in which the polypeptide folds into its final protein
shape or can add additional chemical groups to it. These modifications can inhibit or activate
its function.
Understanding checkpoint: The regulation of protein synthesis

1. What are transcription factors, and what is their role in protein synthesis in eukaryotes?
Before transcription can begin in eukaryotes, a protein called an initiation factor

binds to the promoter region. This facilitates the binding of other transcription
factors that stabilize the RNA polymerase to help it bind to the correct starting
codon on the mRNA transcript. The transcription factors can either inhibit or
stimulate the transcription process.
2. What is an operon and why is it considered an efficient way to regulate genes?
An operon is a group of genes that are regulated by one regulatory protein. The
genes in the operon are expressed together or not at all. This is an efficient way
to regulate genes that are involved in the same biochemical pathway because
only one regulatory protein is needed instead of several—one each, to control
each gene.
3. Describe one example of positive regulation in an operon.
When glucose levels are low in a cell, an activator protein will bind to a site
close to the promoter (Plac) region on the lac operon. This makes it easier for
the RNA polymerase to bind to the promoter so that the lac genes will be
transcribed at a higher rate, which will ultimately result in more glucose for the
cell.
Mutations
Imagine that you tried to copy the text of this entire course, word for word, into your
notebook. How many mistakes do you think you would make? Don’t feel bad because, as it
turns out, cells make errors too, while copying DNA—millions of them per second! These
errors are called mutations.
Mutation or errors in DNA can also be caused by:
Mutagens, which are environmental factors (for example, UV light)
Chemical agents that are able to change the nucleotide sequence in DNA.
Your genetic code is potentially full of mutations caused by copying errors and mutagens.
Fortunately, cells can repair these mutations, to some extent.
Mutations in your DNA blueprint may change the amino acid sequence in polypeptides and
may possibly cause a change in proteins as well. Depending on the proteins involved, these
errors could either have no effect, or could lead to serious diseases, such as cancer.
Errors can also be made during transcription, when RNA polymerase accidently adds the
wrong RNA nucleotide to the mRNA strand. Fortunately, there are usually enough correct
copies of the mRNA produced to ensure that enough of the correctly translated proteins are
made.
Mutations that occur only in the body cells are called somatic cell mutations. These
mutations are not passed on to offspring but are replicated as the organism replaces its own
cells. Although these mutations are potentially dangerous, they only affect that individual.
When mutations occur in the sex cells, they have the potential to be passed on to the next
generation. These are called germ cell mutations. Mutations in germ cells can have serious
consequences for successive generations. Diseases such as sickle-cell anemia, hemophilia,
and various cancers are all examples of the effect of inherited harmful mutations.
Mutations are not always harmful; they are actually a key source of genetic variation upon
which natural selection can act. Genetic variation is important as it creates new traits to be
tested in nature and is the ultimate source of new variations to drive evolution.
There are essentially two classes of mutations:
Gene-level mutations: mistakes in the base-pair sequence of genes

Chromosome-level mutations: are mistakes in the arrangement or number of genes
on a chromosome.
Both are described in more detail in the next sections.
Discover more: Optional Video
If you’d like, Explore the following optional video to preview DNA

Mutations in terms of gene-level and chromosome-level mutations
(https://www.youtube.com/watch?v=eDbK0cxKKsk&feature=youtu.be) or
perform your own research on the topic.
Gene-level mutations
Mutations within a gene happen when one or more bases are replaced with the wrong
nucleotides. The effect of this mutation can range from no effect, all the way up to a complete
misreading of the entire gene. This level of mutation only affects the one gene.
There are two major types of gene-level mutations:
Point Mutations (Substitution Mutations)

Frameshift Mutations
To help you understand how they work, here is a DNA coding sequence for a normal
segment of insulin. You will see how various gene-level mutations change the way that this
coding sequence is translated into proteins.
DNA CCC TAT CAT GTT GTC ACA ACG CGG

codon
mRNA GGG AUA GUA CAA CAG UGU UGC GCC

codon
Amino Glycine Isoleucine Valine Glutamate Glutamate Cystine Cystine Alanine

acid
Point Mutations (Substitution Mutations)
A point mutation involves the substitution of one nucleotide, but it only affects the codon in
which it occurs. It has no effect on neighbouring codons in the gene.
There are three types of gene-level point mutation, which are substitution mutations, based
on their impact on the polypeptide produced:
Silent
Missense
Nonsense mutations

Silent Mutations
This occurs when there is a mutation in one nucleotide, but because of the
redundancy of the genetic code, there is no change of amino acid. As a result, there
is no effect on the resulting polypeptide. For example, there is a mutation in the
second codon. The third base is changed from a T to a G. This changes the mRNA
codon from AUA to AUC. However, the same amino acid (isoleucine) is still
produced.
Part of the coding sequence that results in a NORMAL segment of insulin:

codon

codon

acid
SILENT MUTATION in the second codon of a segment of insulin:
DNA CCC TAG CAT GTT GTC ACA ACG CGG

codon
mRNA GGG AUC GUA CAA CAG UGU UGC GCC

codon

acid

Missense Mutations
A missense mutation occurs when a nucleotide substitution results in the

replacement of one amino acid in the polypeptide chain. Even changing one amino
acid can have drastic effects on the structure of the polypeptide (as you saw in the
example of sickle-cell anemia ß-hemoglobin at the beginning of this learning activity).
Part of the coding sequence that results in a normal segment of insulin:

codon

codon

acid
Missense mutation in the sixth codon of a segment of insulin:
DNA CCC TAT CAT GTT GTC ACC ACG CGG

codon
mRNA GGG AUA GUA CAA CAG UGG UGC GCC

codon
Amino Glycine Isoleucine Valine Glutamate Glutamate Tryptophan Cystine Alanine

acid

Nonsense Mutations
A nonsense mutation occurs when a nucleotide substitution results in an amino acid

codon changing to a STOP codon. The result is that elongation is stopped; the
polypeptide is too short, and so is non-functional.

codon

codon

acid
Nonsense mutation in the sixth codon of a segment of insulin:
DNA CCC TAT CAT GTT GTC ACT ACG CGG

codon
mRNA GGG AUA GUA CAA CAG UGA UGC GCC

codon
Amino Glycine Isoleucine Valine Glutamate Glutamate STOP Not

acid translated
Frameshift Mutations
The insertion or deletion of a nucleotide can cause the entire reading frame of the gene to be
shifted. Neighbouring codons are all affected.

Insertion of a Nucleotide
Adding a single nucleotide to the sequence can result in a frameshift mutation. The
mRNA sequence will now be wrong from the point where the insertion occurred, to
the end of the gene. For example, the insertion of one additional nucleotide (C in the
DNA codon CAC) causes all of the other codons in the gene to be misread by
moving every letter one position over to the right.

codon

codon

acid
Insertion of an additional nucleotide (C) in the last position of the third codon. All of
the codons after that are misread, with their changes shown in bold.
DNA CCC TAT CAC TGT TGT CAC AAC GCG

codon
mRNA GGG AUA GUG ACA ACA GUG UUG CGC

codon
Amino Glycine Isoleucine Valine Threonine Threonine Valine Leucine Arginine

acid

Deletion of a Nucleotide
Removing a single nucleotide from the sequence can also result in a frameshift
mutation. The mRNA sequence will now be wrong from the point where the deletion
occurred, to the end of the gene. For example, the deletion of one nucleotide causes
all of the other codons in the gene to be misread by moving every letter one position
over to the left.

codon

codon

acid
Deletion of a single nucleotide (T) in the last position of the third codon. All of the
other codons after that are misread, with the changes shown in bold:
DNA CCC TAT CAG TTG TCA CAA CGC GG…

codon
mRNA GGG AUA GUC AAC AGU GUU GCG CC…

codon
Amino Glycine Isoleucine Valine Asparagine Serine Glutamate Alanine ?

acid
Chromosome-level mutations
Mutations in the structure of the chromosome can affect many genes. These mutations occur
during meiosis. Chromosomal mutations can produce rapid genetic changes that lead to the
development of new species.
There are two types of chromosome-level mutations:
Translocation
Inversion.
Translocation
This occurs when there is a relocation of groups of base pairs from one part of the
chromosome to the other. It was thought that genes were fixed in one predictable location on
the chromosome. Barbara McClintock’s discovery in the late 1940s that genes could move
from one location to another within the genome was quite surprising. In 1983, Dr. McClintock
was awarded the Nobel Prize in Physiology/Medicine for her discovery of short segments of
moveable DNA, known as transposons. Many of these translocations occur normally within
meiotic division.
Inversion
This occurs when a segment on the chromosome is cut out, and then turned around and
reinserted backwards. The result is that it has reversed its orientation in the chromosome by
flipping from 5’ – 3’ to 3’ – 5’. This also happens during meiosis.
Understanding checkpoint: Protein synthesis
The following table presents the first few codons from a normal DNA
sequence, as well as its corresponding mRNA and amino acid sequences for
a hypothetical polypeptide. You will use the information in this table to answer
the following set of questions.
DNA TAC TGG CTA ATG TCG AAA CCG

codon
(5´–3´)
mRNA AUG ACC GAU UAC AGC UUU GGC

codon
Amino Methionine Threonine Asparagine Tryptophan Serine Phenylalanine Glycine

acid
a) The fourth DNA codon, ATG, has a substitution of its third nucleotide, G, for a T, so it
becomes ATT. Determine the change in the DNA codon, mRNA codon and amino acid
produced by this change.
DNA codon TAC TGG CTA ATT

(5´–3´)
mRNA codon AUG ACC GAU UAA
Amino acid Methionine Threonine Asparagine Stop
Show Answers
Describe and explain the changes.
The new fourth DNA codon would be ATT. This would be transcribed as UAA,
which is the STOP codon. This would cause a nonsense mutation, as the
polypeptide would be too short.
b) The fifth DNA codon, TCG, has an insertion of a G between its first and second
nucleotides, so it becomes TGC.
DNA codon TAC TGG CTA ATG TCG

(5´–3´) TGC
mRNA AUG ACC GAU UAC ACG

codon
Amino acid Methionine Threonine Asparagine Tryptophan Threonine
Show Answers
Describe and explain the changes:
The new fifth DNA codon would be TGC and the reading frame would be shifted
one letter to the right. This would cause completely new codons to be read, from
then on. All the amino acids from the fifth codon onwards would likely be
different from what they were supposed to be, resulting in a missense mutation.
c) The sixth DNA codon has a substitution of its third nucleotide, A, for G, so it becomes
AAG.
DNA TAC TGG CTA ATG TCG AAA

codon AAG
(5´–3´)
mRNA AUG ACC GAU UAC AGC UUC

codon
Amino Methionine Threonine Aspargine Tryptophan Serine Phenylalanine

acid
Show Answers
Describe and explain the changes:
The new sixth DNA codon would be AAG. This would change the mRNA codon
from UUU to UUC, but due to redundancy in the genetic code, both of these
mRNA codons would code for the same amino acid, phenylalanine. This results
in a silent mutation, because there would be no change in the polypeptide.
Part 1: Vocabulary list

This learning activity contains a lot of new terms. Create a vocabulary list for yourself to help
you study and practice concepts. Create a brief definition for each of the terms below.
Nucleic acids Amino acid
Codon Protein synthesis
Genes Gene expression
Transcription Translation
mRNA Central dogma of genetics
Polypeptide Regulatory Region
Transcribed Region RNA Polymerase
mRNA destroyer Template strand (DNA)
Promoter sequence Transcription bubble
Endonucleases GC Hairpin (termination
GTP protective cap (5’ end) Poly-A tail
Intron Extron
Spliceosomes Ribosomes
tRNA Initiation complex
Aminoacyl-tRNA synthetase Start codon
Ribosome active site Stop codon
Transcription factors Operon
Control region Gene-level mutations
Chromosome-level mutations Point mutations
Frameshift mutations Translocation
Inversion
Part 2: Reflection
Now that you have completed this learning activity, reflect on the success criteria.
use appropriate terminology related to protein synthesis

compare the structures and functions of RNA and DNA, and explain their roles in the
process of protein synthesis
investigate the process of protein synthesis using interactive simulations
explain and order the steps involved in the process of protein synthesis
compare how genetic expression is controlled in prokaryotes and eukaryotes by
regulatory proteins
explain how mutagens, such as radiation and chemicals, can cause mutations by
changing the genetic material in cells
Looking at your notes for this learning activity, are they complete? Do you have all the
information you will need to study later on? Take the time to review concepts you are unsure
about before moving on.
Select your level of readiness for each criterion.
Yes - Not yet - need to

Success Criteria confident I review the learning
am able activity
use appropriate terminology related to protein

synthesis
compare the structures and functions of RNA and

DNA, and explain their roles in the process of
protein synthesis
investigate the process of protein synthesis using

interactive simulations
explain and order the steps involved in the

process of protein synthesis
compare how genetic expression is controlled in

prokaryotes and eukaryotes by regulatory
proteins
explain how mutagens, such as radiation and

chemicals, can cause mutations by changing the
genetic material in cells

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9/16/24, 12:34 PM Learning activity 4.

3: Exploring protein synthesis

How many different letters do you notice in the image above?

Decode the following messages in your notebook before checking the

Hide Suggested Answer

Answer: Decoding DNA is fun.

Hide Suggested Answer

Answer: Human DNA contains 3 billion base pairs.

Hide Suggested Answer

The importance of protein synthesis

Understanding checkpoint: The importance of protein synthesis

 You are correct. All of the statements answer the question.

Overview of the protein synthesis process

The two main stages in Protein Synthesis are:

Overview of the process of protein synthesis in eukaryotes. DNA is transcribed into

The “central dogma” of genetics

Early research into protein synthesis

One gene-one polypeptide hypothesis

How mutations cause disease

those with a genetic disease called sickle-cell anemia.

Discovering the genetic code

First letter U C A G Third letter

U Phenylalanine Serine Tyrosine Cysteine U

Phenylalanine Serine Tyrosine Cysteine C

Leucine Serine STOP STOP A

Leucine Serine STOP Tryptophan G

C Leucine Proline Histidine Arginine U

Leucine Proline Histidine Arginine C

Leucine Proline Glutamine Arginine A

Leucine Proline Glutamine Arginine G

A Isoleucine Threonine Asparagine Serine U

Isoleucine Threonine Asparagine Serine C

Isoleucine Threonine Lysine Arginine A

START/Methionine Threonine Lysine Arginine G

G Valine Alanine Aspartate Glycine U

Valine Alanine Aspartate Glycine C

Valine Alanine Glutamate Glycine A

Valine Alanine Glutamate Glycine G

Write a codon for Lysine.

Hide Suggested Answer

Codon 1: AAA or Codon 2: AAG

Understanding checkpoint: The genetic code

 Yes, this is correct. Transcription occurs in the nucleus.

DNA codon (5 - TAC TAG AAA TCT GCG ATG ATT

mRNA codon AUG AUC UUU AGA CGC UAC UAA

 Yes, this is exactly what the ‘central dogma’ of genetics states.

Hide Suggested Answer

individual amino acids that make up one of the β-hemoglobin

Hide Suggested Answer

1. What are genes?

2. Summarize transcription and translation.

3. What type of RNA have you already learned about?

1. Enter by clicking on the “Expression” tab

2. Take a look at Gene 1. What type of macromolecule do you think it is (protein,

Show Suggested Answer

Show Suggested Answer

4. Drag the RNA polymerase back to the tool box.

7. Record your observations

8. Make notes on the purpose/roles of the regulatory region, positive transcription

1. Click “Next Gene” to move to gene 2