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    Protien Synthesis Elongation & Termination

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    vesasc
    The document summarizes the process of elongation during protein synthesis. It describes the three phases of elongation: aminoacyl-tRNA binding to the A site, transpeptidation where the growing polypeptide chain is transferred to the amino acid in the A site, and translocation where the ribosome moves along the mRNA. Elongation factors EF-Tu, EF-Ts, and EF-G are involved in bringing aminoacyl-tRNAs to the A site and facilitating translocation. Elongation continues until a stop codon is reached, leading to termination and release of the completed protein.

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    Protien Synthesis Elongation & Termination

    Uploaded by

    vesasc
    45 views14 pages
    The document summarizes the process of elongation during protein synthesis. It describes the three phases of elongation: aminoacyl-tRNA binding to the A site, transpeptidation where the growing polypeptide chain is transferred to the amino acid in the A site, and translocation where the ribosome moves along the mRNA. Elongation factors EF-Tu, EF-Ts, and EF-G are involved in bringing aminoacyl-tRNAs to the A site and facilitating translocation. Elongation continues until a stop codon is reached, leading to termination and release of the completed protein.

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    PROTIEN SYNTHESIS

    Original Title

    PROTIEN SYNTHESIS ELONGATION & TERMINATION

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    The document summarizes the process of elongation during protein synthesis. It describes the three phases of elongation: aminoacyl-tRNA binding to the A site, transpeptidation where the growing polypeptide chain is transferred to the amino acid in the A site, and translocation where the ribosome moves along the mRNA. Elongation factors EF-Tu, EF-Ts, and EF-G are involved in bringing aminoacyl-tRNAs to the A site and facilitating translocation. Elongation continues until a stop codon is reached, leading to termination and release of the completed protein.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PPTX, PDF, TXT or read online from Scribd
    Download as pptx, pdf, or txt
    45 views14 pages

    Protien Synthesis Elongation & Termination

    Uploaded by

    vesasc
    The document summarizes the process of elongation during protein synthesis. It describes the three phases of elongation: aminoacyl-tRNA binding to the A site, transpeptidation where the growing polypeptide chain is transferred to the amino acid in the A site, and translocation where the ribosome moves along the mRNA. Elongation factors EF-Tu, EF-Ts, and EF-G are involved in bringing aminoacyl-tRNAs to the A site and facilitating translocation. Elongation continues until a stop codon is reached, leading to termination and release of the completed protein.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PPTX, PDF, TXT or read online from Scribd
    Download as pptx, pdf, or txt
    of 14

    PRESENTED BY: MS.PRAMILA JOG (SY.MICRO-145) MS. PRAJAKTA JAMSHETKAR (SY.MICRO-125) V.E.

    S COLLEGE OF ARTS SCIENCE & COMMERCE

    INTRODUCTION:
    In protein synthesis activation and initiation is followed by Elongation of polypeptide chains and termination of polypeptide chains. The elongation cycle is in three phases: -Phase I : Aminoacyl-tRNA binding phase -Phase II : Transpeptidation -Phase III : Translocation Elongation continues until the ribosome adds last amino acid coded by mRNA. Final amino acid is followed by termination codons i.e. UAA, UAG, UGA .

    (A) ELONGATION OF Aminoacyl-tRNA carries amino acids to the POLYPEPTIDE CHAIN ribosome.

    Ribosomes has three sites for binding tRNA 1) P site : Peptidyl or Donor site. In the beginning of elongation, P site is filled with N-formylmethionyl-tRNA (fMet). since its donates amino acid in elongation process to aminoacyl tRNA it is 2) A site : also known as Donor site. Also known as Aminoacyl or acceptor site. (As it accepts aminoacyl tRNA as well as amino acid that is donated by the P site). In the beginning of elongation A site is empty.

    3) E site : Also known as exit site. it is empty.

    Each Aminoacyl-tRNA matches and binds to a specific codon. If the codon does not match, the Aminoacyl-tRNA is rejected. When the anticodon of Aminoacyl-tRNA matches the codon of mRNA in the A-site, it is accepted and binds to mRNA.

    PHASE I: Aminoacyl - tRNA binding phase


    N-formylmethionyl tRNA

    Aminoacyl-tRNA

    Aminoacyl tRNA carrying amino acid is inserted in A site.

    When GTP is bound to elongation factor EF-Tu (elongation factor thermo unstable ) the tRNA is in its active state and delivers aminoacyl This GTP is then hydrolyzed to GDP and EF-Tu. GDP leavesA site. tRNA to the ribosome. (aminoacyl or acceptor site) With help of second elongation factor EF-Ts (thermo stable) , the EfTu.GDP is converted into EF-Tu.GTP which again binds to the

    ( tRNA binds to mRNA)

    PHASE II: Transpeptidation reaction


    In this phase, the amino group of the Asite aminoacyl-tRNA attacks nucleophilically the -carboxyl group of c-terminal amino acid on the P-site tRNA.

    This reaction is catalysed by peptidyl transferase which is located on 50s ribosomal subunit.
    The peptide chain grows by 1 amino acid and it is transferred to A-site.

    PHASE III: Translocation


    Finally, the ribosome translocates along the mRNA thereby moving the new peptidyl-tRNA to the P site and the old (now uncharged) tRNA, which has just lost its Peptidyl chain, to the E site. Translocation is spontaneous after peptide bond formation because the deacylated tRNA in the P site has a higher affinity for the E site, and the peptidyl-tRNA in the A site has a higher affinity for the P site. This step requires the elongation factor, EF-G (also known as translocase).

    GTP is hydrolyzed during translocation and, once again, GTP hydrolysis is required for dissociation of EF-G, not for binding. Also, it releases energy that is used up for movement (translocation). EF-G + GTP EF-G + GDP + Pi
    EF-G blocks the binding of aminoacyl tRNAs to the A site as well as blocking the binding of Release Factors. It effectively makes sure that translocation must take place before the cycle continues. Normally the empty tRNA is released from the E site only after binding of the correct aminoacyl-tRNA at the A site causes a decreased affinity for tRNA in the E site.

    TERMINATION
    -The final phase of protein synthesis requires that the finished polypeptide chain be detached from a tRNA. This can only happen in response to the signal that a stop codon has been reached. After hydrolysis, the ribosome subunits dissociate.

    -The end of the code for the protein in the mRNA is signaled by one of three special codons called stop codons. These stop codons have the sequences UAA, UAG, and UGA.
    Binding of Release factors tRNAs cannot recognize the stop codons. Rather they are recognized by release factor. RF1 - recognizes the UAA and UAG stop codons. RF2 - which recognizes the UAA and UGA stop codons. RF3 (GTP) - stimulates the binding of RF1 and RF2.

    Hydrolysis of the peptidyl-tRNA Binding of the release factors alters the Peptidyl transferase activity so that water is now the nucleophilic attack agent. The result is hydrolysis of the peptidyl-tRNA and release of the completed polypeptide chain. The uncharged tRNA then dissociates as do the release factors. GTP is hydrolyzed. Dissociation Finally, the ribosome dissociates into its 30S and 50S subunits and the mRNA is released. IF3 may help this process.

    References: Prescott & Harley 7th edition Lehninger- 5th edition Dubey www.wikipedia.com www.google.com

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