Lambda phage

Enterobacteria phage λ (lambda phage, coliphage λ, officially

Escherichia virus Lambda) is a bacterial virus, or bacteriophage, Escherichia virus Lambda
that infects the bacterial species Escherichia coli (E. coli). It was
discovered by Esther Lederberg in 1950.[2] The wild type of this
virus has a temperate life cycle that allows it to either reside
within the genome of its host through lysogeny or enter into a
lytic phase, during which it kills and lyses the cell to produce
offspring. Lambda strains, mutated at specific sites, are unable to
lysogenize cells; instead, they grow and enter the lytic cycle after
superinfecting an already lysogenized cell.[3]

The phage particle consists of a head (also known as a capsid),[4]

a tail, and tail fibers (see image of virus below). The head
contains the phage's double-strand linear DNA genome. During
infections, the phage particle recognizes and binds to its host, E.
coli, causing DNA in the head of the phage to be ejected through
the tail into the cytoplasm of the bacterial cell. Usually, a "lytic
cycle" ensues, where the lambda DNA is replicated and new
phage particles are produced within the cell. This is followed by Electron micrograph of a virus particle
cell lysis, releasing the cell contents, including virions that have of species Escherichia virus Lambda
been assembled, into the environment. However, under certain
Virus classification
conditions, the phage DNA may integrate itself into the host cell
chromosome in the lysogenic pathway. In this state, the λ DNA (unranked): Virus
is called a prophage and stays resident within the host's genome
Realm: Duplodnaviria
without apparent harm to the host. The host is termed a lysogen
when a prophage is present. This prophage may enter the lytic Kingdom: Heunggongvirae
cycle when the lysogen enters a stressed condition.
Phylum: Uroviricota

Anatomy Class: Caudoviricetes

Order: Caudovirales
The virus particle consists of a head and a tail that can have tail
Family: Siphoviridae
fibers. The whole particle consists of 12–14 different proteins
with more than 1000 protein molecules total and one DNA Genus: Lambdavirus
molecule located in the phage head. However, it is still not
Species: Escherichia virus
entirely clear whether the L and M proteins are part of the
virion.[5] All characterized lambdoid phages possess an N Lambda
protein-mediated transcription antitermination mechanism, with
the exception of phage HK022.[6]
 Bacteriophage Lambda Structural
Model at Atomic Resolution[1]

Bacteriophage lambda virion (schematic).

Protein names and their copy numbers in
the virion particle are shown. The
presence of the L and M proteins in the
virion is still unclear.[5]
 Linear layout of lambda phage genome with major operons, promoter regions and
capsid coding genes.[5]

The genome contains 48,502[7] base pairs of double-stranded, linear DNA, with 12-base single-strand
segments at both 5' ends.[8] These two single-stranded segments are the "sticky ends" of what is called the
cos site. The cos site circularizes the DNA in the host cytoplasm. In its circular form, the phage genome,
therefore, is 48,502 base pairs in length.[8] The lambda genome can be inserted into the E. coli chromosome
and is then called a prophage. See section below for details.

The tail of lambda phages is made of at least 6 proteins (H, J, U, V, Stf, Tfa) and requires 7 more for
assembly (I, K, L, M, Z, G/T). This assembly process begins with protein J, which then recruits proteins I,
L, K, and G/T to add protein H. Once G and G/T leave the complex, protein V can assemble onto the J/H
scaffold. Then, protein U is added to the head-proximal end of the tail. Protein Z is able to connect the tail
to the head. Protein H is cleaved due to the actions of proteins U and Z.[5]

Life cycle

Infection

Lambda phage is a non-

contractile tailed phage,
meaning during an infection
event it cannot 'force' its DNA
through a bacterial cell
membrane. It must instead use
an existing pathway to invade
the host cell, having evolved
the tip of its tail to interact with
a specific pore to allow entry
of its DNA to the hosts.

1. Bacteriophage Lambda
binds to an E. coli cell
by means of its J protein
in the tail tip. The J
protein interacts with the
maltose outer Lambda phage J protein interaction with the LamB porin
membrane porin (the
product of the lamB
gene) of E. coli,[9] a porin molecule, which is part of the maltose operon.
2. The linear phage genome is injected through the outer membrane.
3. The DNA passes through the mannose permease complex in the inner membrane[10][11]
(encoded by the manXYZ genes) and immediately circularises using the cos sites, 12-base
G-C-rich cohesive "sticky ends". The single-strand viral DNA ends are ligated by host DNA
ligase. It is not generally appreciated that the 12 bp lambda cohesive ends were the subject
of the first direct nucleotide sequencing of a biological DNA.[6]

1. Host DNA gyrase puts negative

supercoils in the circular chromosome,
causing A-T-rich regions to unwind
and drive transcription.
2. Transcription starts from the
constitutive PL, PR and PR' promoters
producing the 'immediate early'
transcripts. At first, these express the N
and cro genes, producing N, Cro and
a short inactive protein.
1. Cro binds to OR3, preventing access
to the PRM promoter, preventing
expression of the cI gene. N binds to
the two Nut (N utilisation) sites, one in
Lambda phage DNA injection into the cell membrane using
the N gene in the PL reading frame, Mannose PTS permease (a sugar transporting system) as
and one in the cro gene in the PR a mechanism of entry into the cytoplasm
reading frame.
2. The N protein is an antiterminator, and
functions by engaging the transcribing RNA polymerase at
specific sites of the nascently transcribed mRNA. When
RNA polymerase transcribes these regions, it recruits N and
forms a complex with several host Nus proteins. This
complex skips through most termination sequences. The
extended transcripts (the 'late early' transcripts) include the
N and cro genes along with cII and cIII genes, and xis, int,
O, P and Q genes discussed later.
3. The cIII protein acts to protect the cII protein from proteolysis
by FtsH (a membrane-bound essential E. coli protease) by
acting as a competitive inhibitor. This inhibition can induce
a bacteriostatic state, which favours lysogeny. cIII also
directly stabilises the cII protein.[12]
Early activation events involving
N protein
On initial infection, the stability of cII determines the lifestyle of the phage; stable cII will lead to the
lysogenic pathway, whereas if cII is degraded the phage will go into the lytic pathway. Low temperature,
starvation of the cells and high multiplicity of infection (MOI) are known to favor lysogeny (see later
discussion).

N antitermination

N Antitermination requires the assembly of a large ribonucleoprotein complex to effectively prolong the anti-
termination process, without the full complex the RNA polymerase is able to bypass only a single terminator[13]

This occurs without the N protein interacting with the DNA; the protein instead binds to the freshly
transcribed mRNA. Nut sites contain 3 conserved "boxes", of which only BoxB is essential.

1. The boxB RNA sequences are located close to the 5' end of the pL and pR transcripts. When
transcribed, each sequence forms a hairpin loop structure that the N protein can bind to.
2. N protein binds to boxB in each transcript, and contacts the transcribing RNA polymerase via
RNA looping. The N-RNAP complex is stabilized by subsequent binding of several host Nus
(N utilisation substance) proteins (which include transcription termination/antitermination
factors and, bizarrely, a ribosome subunit).
3. The entire complex (including the bound Nut site on the mRNA) continues transcription, and
can skip through termination sequences.

Lytic life cycle

This is the lifecycle that the phage follows following most infections, where the cII protein does not reach a
high enough concentration due to degradation, so does not activate its promoters.
 1. The 'late early' transcripts continue being written,
including xis, int, Q and genes for replication of the
lambda genome (OP). Cro dominates the repressor site
(see "Repressor" section), repressing synthesis from the
PRM promoter (which is a promoter of the lysogenic
cycle).
2. The O and P proteins initiate replication of the phage
chromosome (see "Lytic Replication").
3. Q, another antiterminator, binds to Qut sites.
4. Transcription from the PR' promoter can now extend to
produce mRNA for the lysis and the head and tail
proteins.
5. Structural proteins and phage genomes self-assemble Lysis plaques of lambda phage on E.
into new phage particles. coli bacteria
6. Products of the genes S,R, Rz and Rz1 cause cell lysis.
S is a holin, a small membrane protein that, at a time
determined by the sequence of the protein, suddenly makes holes in the membrane. R is an
endolysin, an enzyme that escapes through the S holes and cleaves the cell wall. Rz and
Rz1 are membrane proteins that form a complex that somehow destroys the outer
membrane, after the endolysin has degraded the cell wall. For wild-type lambda, lysis occurs
at about 50 minutes after the start of infection and releases around 100 virions.

Rightward transcription

Rightward transcription expresses the O, P and Q genes. O and P are responsible for initiating replication,
and Q is another antiterminator that allows the expression of head, tail, and lysis genes from PR’.[6]

Pr is the promoter for rightward transcription, and the cro gene is a regulator gene. The cro gene will
encode for the Cro protein that will then repress Prm promoter. Once Pr transcription is underway the Q
gene will then be transcribed at the far end of the operon for rightward transcription. The Q gene is a
regulator gene found on this operon, which will control the expression of later genes for rightward
transcription. Once the gene's regulatory proteins allow for expression, the Q protein will then act as an
anti-terminator. This will then allow for the rest of the operon to be read through until it reaches the
transcription terminator. Thus allowing expression of later genes in the operon, and leading to the
expression of the lytic cycle.[14]

Pr promoter has been found to activate the origin in the use of rightward transcription, but the whole picture
of this is still somewhat misunderstood. Given there are some caveats to this, for instance this process is
different for other phages such as N15 phage, which may encode for DNA polymerase. Another example is
the P22 phage may replace the p gene, which encodes for an essential replication protein for something that
is capable of encoding for a DnaB helices.[6]

Lytic replication
1. For the first few replication cycles, the lambda genome undergoes θ replication (circle-to-
circle).
2. This is initiated at the ori site located in the O gene. O protein binds the ori site, and P protein
binds the DnaB subunit of the host replication machinery as well as binding O. This
effectively commandeers the host DNA polymerase.
3. Soon, the phage switches to a rolling circle replication similar to that used by phage M13.
The DNA is nicked and the 3’ end serves as a primer. Note that this does not release single
 copies of the phage genome but rather one long molecule with many copies of the genome:
a concatemer.
4. These concatemers are cleaved at their cos sites as they are packaged. Packaging cannot
occur from circular phage DNA, only from concatomeric DNA.

Q antitermination

The Q protein modifies the RNA polymerase at the promoter region and is recruited to RNA polymerase. The Q
protein turns into a RNA polymerase subunit after it is recruitment to RNAP and modifies the enzyme into a
processive state. Note that NusA can stimulate the activity of the Q protein.[13]
Q is similar to N in its effect: Q binds to RNA polymerase in Qut sites and the resulting complex can ignore
terminators, however the mechanism is very different; the Q protein first associates with a DNA sequence
rather than an mRNA sequence.[15]

1. The Qut site is very close to the PR’ promoter, close enough that the σ factor has not been
released from the RNA polymerase holoenzyme. Part of the Qut site resembles the -10
Pribnow box, causing the holoenzyme to pause.
2. Q protein then binds and displaces part of the σ factor and transcription re-initiates.
3. The head and tail genes are transcribed and the corresponding proteins self-assemble.

Leftward transcription

Leftward transcription expresses the gam, xis, bar and

int genes.[6] Gam proteins are involved in
recombination. Gam is also important in that it inhibits
the host RecBCD nuclease from degrading the 3’ ends
in rolling circle replication. Int and xis are integration
and excision proteins vital to lysogeny.

Leftward transcription process

1. Lambda phage inserts chromosome into the
Diagram showing the retro-regulation process that
cytoplasm of the host bacterial cell.
yields a higher concentration of xis compared to
2. The phage chromosome is inserted to the int. The mRNA transcript is digested by bacterial
host bacterial chromosome through DNA RNase starting from the cleaved hairpin loop at
ligase. sib.
3. Transcription of the phage chromosome
proceeds leftward when the host RNA
polymerase attaches to promotor site pL resulting in the translation of gene N.
1. Gene N acts a regulatory gene that results in RNA polymerase to be unable to recognize
translation-termination sites.[16]

Leftward Transcription mutations

Leftward transcription is believed to result in a deletion mutation of the rap gene resulting in a lack of
growth of lambda phage. This is due to RNA polymerase attaching to pL promoter site instead of the pR
promotor site. Leftward transcription results in barI and barII transcription on the left operon. Bar positive
phenotype is present when the rap gene is absent. The lack of growth of lambda phage is believed to occur
due to a temperature sensitivity resulting in inhibition of growth.[17]

xis and int regulation of insertion and excision

1. xis and int are found on the same piece of mRNA, so approximately equal concentrations of
xis and int proteins are produced. This results (initially) in the excision of any inserted
genomes from the host genome.
2. The mRNA from the PL promoter forms a stable secondary structure with a stem-loop in the
sib section of the mRNA. This targets the 3' (sib) end of the mRNA for RNAaseIII
degradation, which results in a lower effective concentration of int mRNA than xis mRNA (as
 the int cistron is nearer to the sib sequence than the xis cistron is to the sib sequence), so a
higher concentrations of xis than int is observed.
3. Higher concentrations of xis than int result in no insertion or excision of phage genomes, the
evolutionarily favoured action - leaving any pre-inserted phage genomes inserted (so
reducing competition) and preventing the insertion of the phage genome into the genome of
a doomed host.

Lysogenic (or lysenogenic) life cycle

The lysogenic lifecycle begins once the cI protein reaches a high enough concentration to activate its
promoters, after a small number of infections.

1. The 'late early' transcripts continue being written, including xis, int, Q and genes for
replication of the lambda genome.
2. The stabilized cII acts to promote transcription from the PRE, PI and Pantiq promoters.
3. The Pantiq promoter produces antisense mRNA to the Q gene message of the PR promoter
transcript, thereby switching off Q production. The PRE promoter produces antisense mRNA
to the cro section of the PR promoter transcript, turning down cro production, and has a
transcript of the cI gene. This is expressed, turning on cI repressor production. The PI
promoter expresses the int gene, resulting in high concentrations of Int protein. This int
protein integrates the phage DNA into the host chromosome (see "Prophage Integration").
4. No Q results in no extension of the PR' promoter's reading frame, so no lytic or structural
proteins are made. Elevated levels of int (much higher than that of xis) result in the insertion
of the lambda genome into the hosts genome (see diagram). Production of cI leads to the
binding of cI to the OR1 and OR2 sites in the PR promoter, turning off cro and other early
gene expression. cI also binds to the PL promoter, turning off transcription there too.
5. Lack of cro leaves the OR3 site unbound, so transcription from the PRM promoter may occur,
maintaining levels of cI.
6. Lack of transcription from the PL and PR promoters leads to no further production of cII and
cIII.
7. As cII and cIII concentrations decrease, transcription from the Pantiq, PRE and PI stop being
promoted since they are no longer needed.
8. Only the PRM and PR' promoters are left active, the former producing cI protein and the latter
a short inactive transcript. The genome remains inserted into the host genome in a dormant
state.

The prophage is duplicated with every subsequent cell division of the host. The phage genes expressed in
this dormant state code for proteins that repress expression of other phage genes (such as the structural and
lysis genes) in order to prevent entry into the lytic cycle. These repressive proteins are broken down when
the host cell is under stress, resulting in the expression of the repressed phage genes. Stress can be from
starvation, poisons (like antibiotics), or other factors that can damage or destroy the host. In response to
stress, the activated prophage is excised from the DNA of the host cell by one of the newly expressed gene
products and enters its lytic pathway.

Prophage integration

The integration of phage λ takes place at a special attachment site in the bacterial and phage genomes,
called attλ. The sequence of the bacterial att site is called attB, between the gal and bio operons, and
consists of the parts B-O-B', whereas the complementary sequence in the circular phage genome is called
attP and consists of the parts P-O-P'. The integration itself is a sequential exchange (see genetic
recombination) via a Holliday junction and requires both the phage protein Int and the bacterial protein IHF
(integration host factor). Both Int and IHF bind to attP and form an intasome, a DNA-protein-complex
designed for site-specific recombination of the phage and host DNA. The original B-O-B' sequence is
changed by the integration to B-O-P'-phage DNA-P-O-B'. The phage DNA is now part of the host's
genome.[18]

Maintenance of lysogeny
Lysogeny is maintained solely
by cI. cI represses transcription
from PL and PR while
upregulating and controlling its
own expression from PRM. It is
therefore the only protein
expressed by lysogenic phage.
This is coordinated by the PL
and PR operators. Both
operators have three binding
sites for cI: OL1, OL2, and OL3
for PL, and OR1, OR2 and OR3
for PR.
cI binds most favorably to OR1; A simplified representation of the integration/excision paradigm
binding here inhibits and the major genes involved.
transcription from PR. As cI
easily dimerises, the binding of
cI to OR1 greatly increases the affinity of the binding of cI
to OR2, and this happens almost immediately after OR1
binding. This activates transcription in the other direction
from PRM, as the N terminal domain of cI on OR2 tightens
the binding of RNA polymerase to PRM and hence cI Lysogen repressors and polymerase
stimulates its own transcription. When it is present at a bound to OR1 and recruits OR2,
much higher concentration, it also binds to OR3, which will activate PRM and
inhibiting transcription from PRM, thus regulating its own shutdown PR.
levels in a negative feedback loop.
cI binding to the PL operator is very similar, except that it
has no direct effect on cI transcription. As an additional repression of its own expression,
however, cI dimers bound to OR3 and OL3 bend the DNA between them to tetramerise.
The presence of cI causes immunity to superinfection by other lambda phages, as it will
inhibit their PL and PR promoters.

Induction

The classic induction of a lysogen involved irradiating the infected cells with UV light. Any situation where
a lysogen undergoes DNA damage or the SOS response of the host is otherwise stimulated leads to
induction.

1. The host cell, containing a dormant phage genome, experiences DNA damage due to a high
stress environment, and starts to undergo the SOS response.
 2. RecA (a cellular protein) detects DNA damage and
becomes activated. It is now RecA*, a highly specific co-
protease.
3. Normally RecA* binds LexA (a transcription repressor),
activating LexA auto-protease activity, which destroys LexA
repressor, allowing production of DNA repair proteins. In
lysogenic cells, this response is hijacked, and RecA*
stimulates cI autocleavage. This is because cI mimics the
structure of LexA at the autocleavage site.
4. Cleaved cI can no longer dimerise, and loses its affinity for
DNA binding.
5. The PR and PL promoters are no longer repressed and
switch on, and the cell returns to the lytic sequence of
expression events (note that cII is not stable in cells Transcriptional state of the PRM
undergoing the SOS response). There is however one and PR promoter regions during a
notable difference. lysogenic state vs induced, early
lytic state.

Control of phage genome excision in induction

1. The phage genome is still inserted in the host genome and
needs excision for DNA replication to occur. The sib section
beyond the normal PL promoter transcript is, however, no
longer included in this reading frame (see diagram).
2. No sib domain on the PL promoter mRNA results in no
hairpin loop on the 3' end, and the transcript is no longer
targeted for RNAaseIII degradation.
3. The new intact transcript has one copy of both xis and int, The function of LexA in the SOS
so approximately equal concentrations of xis and int response. LexA expression leads
proteins are produced.
to inhibition of various genes
4. Equal concentrations of xis and int result in the excision of including LexA.
the inserted genome from the host genome for replication
and later phage production.

Multiplicity reactivation and prophage reactivation

Multiplicity reactivation (MR) is the process by which multiple viral genomes, each containing inactivating
genome damage, interact within an infected cell to form a viable viral genome. MR was originally
discovered with phage T4, but was subsequently found in phage λ (as well as in numerous other bacterial
and mammalian viruses[19]). MR of phage λ inactivated by UV light depends on the recombination
function of either the host or of the infecting phage.[20] Absence of both recombination systems leads to a
loss of MR.

Survival of UV-irradiated phage λ is increased when the E. coli host is lysogenic for an homologous
prophage, a phenomenon termed prophage reactivation.[21] Prophage reactivation in phage λ appears to
occur by a recombinational repair process similar to that of MR.

Repressor
The repressor found in the phage lambda is a notable example of
the level of control possible over gene expression by a very simple
system. It forms a 'binary switch' with two genes under mutually
exclusive expression, as discovered by Barbara J. Meyer.[22]

The lambda repressor gene system consists of (from left to right on

the chromosome):

cI gene Protein interactions that lead to

OR3 either Lytic or Lysogenic cycles for
OR2 Lambda phage

OR1
cro gene

The lambda repressor is a self

assembling dimer also known as the cI
protein.[23] It binds DNA in the helix-
turn-helix binding motif. It regulates the
transcription of the cI protein and the
Cro protein.

The life cycle of lambda phages is

controlled by cI and Cro proteins. The
lambda phage will remain in the
lysogenic state if cI proteins
predominate, but will be transformed
into the lytic cycle if cro proteins
predominate.

The cI dimer may bind to any of three

operators, OR1, OR2, and OR3, in the
order OR1 > OR2 > OR3. Binding of a Visual representation of repressor tetramer/octamer binding to
cI dimer to OR1 enhances binding of a phage lambda L and R operator sites (stable lysogenic state)
second cI dimer to OR2, an effect called
cooperativity. Thus, OR1 and OR2 are
almost always simultaneously occupied by cI. However, this does not increase the affinity between cI and
OR3, which will be occupied only when the cI concentration is high.

At high concentrations of cI, the dimers will also bind to operators OL1 and OL2 (which are over 2 kb
downstream from the R operators). When cI dimers are bound to OL1, OL2, OR1, and OR2 a loop is
induced in the DNA, allowing these dimers to bind together to form an octamer. This is a phenomenon
called long-range cooperativity. Upon formation of the octamer, cI dimers may cooperatively bind to OL3
and OR3, repressing transcription of cI. This autonegative regulation ensures a stable minimum
concentration of the repressor molecule and, should SOS signals arise, allows for more efficient prophage
induction.[24]

In the absence of cI proteins, the cro gene may be transcribed.

In the presence of cI proteins, only the cI gene may be transcribed.
At high concentration of cI, transcriptions of both genes are repressed.
Some base pairs with Protein cl turned ON, Lysogen repression all
serve a dual function with repressor bound 3 sites bound is a low
with promoter and to OR2 polymerase occurrence due to
operator for either cl binding is increased OR3 weak binding
and cro proteins. and turn OFF OR1. affinity. OR1
repression increases
binding affinity to OR2
due to repressor-
repressor interaction.
Increased
concentrations of
repressor increase
binding.

Protein function overview

Function in life Promoter
Protein Description
cycle region
Regulatory protein
PL (Clear 3) HflB (FtsH) binding protein, protects cII from
cIII CIII. Lysogeny, cII
degradation by proteases.
Stability

(Clear 2) Activates transcription from the PAQ , PRE and

PI promoters, transcribing cI and int. Low stability due
Lysogeny, to susceptibility to cellular HflB (FtsH) proteases
cII Transcription PR (especially in healthy cells and cells undergoing the
activator SOS response). High levels of cII will push the phage
toward integration and lysogeny while low levels of cII
will result in lysis.
(Clear 1) Transcription inhibitor, binds OR1, OR2 and
OR3 (affinity OR1 > OR2 = OR3, i.e. preferentially binds
OR1). At low concentrations blocks the PR promoter
Repressor,
PRM, PRE (preventing cro production). At high concentrations
cI Maintenance of
downregulates its own production through OR3 binding.
Lysogeny
Repressor also inhibits transcription from the PL
promoter. Susceptible to cleavage by RecA* in cells
undergoing the SOS response.
Transcription inhibitor, binds OR3, OR2 and OR1 (affinity
OR3 > OR2 = OR1, i.e. preferentially binds OR3). At low
Lysis, Control of
cro Repressor's PR concentrations blocks the pRM promoter (preventing cI
Operator production). At high concentrations downregulates its
own production through OR2 and OR1 binding. No
cooperative binding (c.f. below for cI binding)

Lysis, DNA PR Replication protein O. Initiates Phage Lambda DNA

O
replication replication by binding at ori site.
 Initiates Phage Lambda DNA replication by binding to O
Lysis, DNA
P PR and DnaB subunit. These bindings provide control over
Replication
the host DNA polymerase.
Lysis, DNA Inhibits host RecBCD nuclease from degrading 3' ends
gam PL
replication —allow rolling circle replication to proceed.

PR' Holin, a membrane protein that perforates the

S Lysis
membrane during lysis.

Endolysin, Lysozyme, an enzyme that exits the cell

R Lysis PR' through the holes produced by Holin and cleaves apart
the cell wall.
Forms a membrane protein complex that destroys the
outer cell membrane following the cell wall degradation
Rz and Rz1 Lysis PR'
by endolysin. Spanin, Rz1(outer membrane subunit) and
Rz(inner membrane subunit).

F Lysis PR' Phage capsid head proteins.

D Lysis PR' Head decoration protein.

E Lysis PR' Major head protein.

C Lysis PR' Minor capsid protein.

B Lysis PR' Portal protein B.

A Lysis PR' Large terminase protein.

J Lysis PR' Host specificity protein J.

MVUGLTZ Lysis PR' Minor tail protein M.

K Lysis PR' Probable endopeptidase.

H Lysis PR' Tail tape measure protein H.

I Lysis PR' Tail assembly protein I.

FI Lysis PR' DNA-packing protein FI.

FII Lysis PR' Tail attachment protein.

tfa Lysis PR' Tail fiber assembly protein.

Integrase, manages insertion of phage genome into the

host's genome. In Conditions of low int concentration
Genome there is no effect. If xis is low in concentration and int
int Integration, P I, P L high then this leads to the insertion of the phage
Excision genome. If xis and int have high (and approximately
equal) concentrations this leads to the excision of
phage genomes from the host's genome.

P I, P L Excisionase and int protein regulator, manages excision

xis Genome Excision
and insertion of phage genome into the host's genome.
Antiterminator, RNA-binding protein and RNA
polymerase cofactor, binds RNA (at Nut sites) and
transfers onto the nascent RNApol that just transcribed
Antitermination for
the nut site. This RNApol modification prevents its
N Transcription of PL
recognition of termination sites, so normal RNA
Late Early Genes
polymerase termination signals are ignored and RNA
synthesis continues into distal phage genes (cII, cIII,
xis, int, O, P, Q)

Q Antitermination for PR Antiterminator, DNA binding protein and RNApol

Transcription of cofactor, binds DNA (at Qut sites) and transfers onto the
 Late Lytic Genes initiating RNApol. This RNApol modification alters its
recognition of termination sequences, so normal ones
are ignored; special Q termination sequences some
20,000 bp away are effective. Q-extended transcripts
include phage structural proteins (A-F, Z-J) and lysis
genes (S, R, Rz and Rz1). Downregulated by Pantiq
antisense mRNA during lysogeny.

DNA repair protein, functions as a co-protease during

RecA SOS Response Host protein SOS response, auto-cleaving LexA and cI and
facilitating lysis.

Lytic vs. lysogenic

An important distinction here is that between the two decisions;
lysogeny and lysis on infection, and continuing lysogeny or lysis
from a prophage. The latter is determined solely by the activation of
RecA in the SOS response of the cell, as detailed in the section on
induction. The former will also be affected by this; a cell
undergoing an SOS response will always be lysed, as no cI protein
will be allowed to build up. However, the initial lytic/lysogenic
decision on infection is also dependent on the cII and cIII proteins. Diagram of temperate phage life
cycle, showing both lytic and
In cells with sufficient nutrients, protease activity is high, which
lysogenic cycles.
breaks down cII. This leads to the lytic lifestyle. In cells with
limited nutrients, protease activity is low, making cII stable. This
leads to the lysogenic lifestyle. cIII appears to stabilize cII, both directly and by acting as a competitive
inhibitor to the relevant proteases. This means that a cell "in trouble", i.e. lacking in nutrients and in a more
dormant state, is more likely to lysogenise. This would be selected for because the phage can now lie
dormant in the bacterium until it falls on better times, and so the phage can create more copies of itself with
the additional resources available and with the more likely proximity of further infectable cells.

A full biophysical model for lambda's lysis-lysogeny decision remains to be developed. Computer modeling
and simulation suggest that random processes during infection drive the selection of lysis or lysogeny within
individual cells.[25] However, recent experiments suggest that physical differences among cells, that exist
prior to infection, predetermine whether a cell will lyse or become a lysogen.[26]

As a genetic tool
Lambda phage has been used heavily as a model organism and has been an excellent tool first in microbial
genetics, and then later in molecular genetics.[27] Some of its uses include its application as a vector for the
cloning of recombinant DNA; the use of its site-specific recombinase (int) for the shuffling of cloned DNAs
by the gateway method;[28] and the application of its Red operon, including the proteins Red alpha (also
called 'exo'), beta and gamma in the DNA engineering method called recombineering. The 48 kb DNA
fragment of lambda phage is not essential for productive infection and can be replaced by foreign DNA,[29]
which can then be replicated by the phage. Lambda phage will enter bacteria more easily than plasmids,
making it a useful vector that can either destroy or become part of the host's DNA.[30] Lambda phage can
also be manipulated and used as an anti-cancer vaccine that targets human aspartyl (asparaginyl) β-
hydroxylase (ASPH, HAAH), which has been shown to be beneficial in cases of hepatocellular carcinoma
in mice.[31] Lambda phage has also been of major importance in the study of specialized transduction.[32]

See also
Esther Lederberg
Lambda holin family
Molecular weight size marker
Sankar Adhya
Zygotic induction
Corynebacteriophages – Corynephages β (beta) and ω (omega) are (proposed) members of
genus Lambdavirus

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Further reading
Watson J, Baker T, Bell S, Gann A, Levine M, Losick R. Molecular Biology of the Gene
(International Edition) (6th ed.).
Ptashne M, Hopkins N (August 1968). "The operators controlled by the lambda phage
repressor" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC224915). Proceedings of the
National Academy of Sciences of the United States of America. 60 (4): 1282–7.
Bibcode:1968PNAS...60.1282P (https://ui.adsabs.harvard.edu/abs/1968PNAS...60.1282P).
doi:10.1073/pnas.60.4.1282 (https://doi.org/10.1073%2Fpnas.60.4.1282). PMC 224915 (http
s://www.ncbi.nlm.nih.gov/pmc/articles/PMC224915). PMID 5244737 (https://pubmed.ncbi.nl
m.nih.gov/5244737).
Meyer BJ, Kleid DG, Ptashne M (December 1975). "Lambda repressor turns off transcription
of its own gene" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC388816). Proceedings of the
National Academy of Sciences of the United States of America. 72 (12): 4785–89.
Bibcode:1975PNAS...72.4785M (https://ui.adsabs.harvard.edu/abs/1975PNAS...72.4785M).
doi:10.1073/pnas.72.12.4785 (https://doi.org/10.1073%2Fpnas.72.12.4785). PMC 388816 (h
ttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC388816). PMID 1061069 (https://pubmed.ncbi.
nlm.nih.gov/1061069).
Brüssow H, Hendrix RW (January 2002). "Phage genomics: small is beautiful" (https://doi.or
g/10.1016%2FS0092-8674%2801%2900637-7). Cell. 108 (1): 13–16. doi:10.1016/S0092-
8674(01)00637-7 (https://doi.org/10.1016%2FS0092-8674%2801%2900637-7).
PMID 11792317 (https://pubmed.ncbi.nlm.nih.gov/11792317).
Dodd IB, Shearwin KE, Egan JB (April 2005). "Revisited gene regulation in bacteriophage
lambda". Current Opinion in Genetics & Development. 15 (2): 145–152.
doi:10.1016/j.gde.2005.02.001 (https://doi.org/10.1016%2Fj.gde.2005.02.001).
PMID 15797197 (https://pubmed.ncbi.nlm.nih.gov/15797197).
Friedman DI, Court DL (April 2001). "Bacteriophage lambda: alive and well and still doing its
thing". Current Opinion in Microbiology. 4 (2): 201–207. doi:10.1016/S1369-5274(00)00189-
2 (https://doi.org/10.1016%2FS1369-5274%2800%2900189-2). PMID 11282477 (https://pub
med.ncbi.nlm.nih.gov/11282477).
 Gottesman ME, Weisberg RA (December 2004). "Little lambda, who made thee?" (https://ww
w.ncbi.nlm.nih.gov/pmc/articles/PMC539004). Microbiology and Molecular Biology Reviews.
68 (4): 796–813. doi:10.1128/MMBR.68.4.796-813.2004 (https://doi.org/10.1128%2FMMBR.
68.4.796-813.2004). PMC 539004 (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC539004).
PMID 15590784 (https://pubmed.ncbi.nlm.nih.gov/15590784).
Hendrix RW, Smith MC, Burns RN, Ford ME, Hatfull GF (March 1999). "Evolutionary
relationships among diverse bacteriophages and prophages: all the world's a phage" (https://
www.ncbi.nlm.nih.gov/pmc/articles/PMC26759). Proceedings of the National Academy of
Sciences of the United States of America. 96 (5): 2192–2197.
Bibcode:1999PNAS...96.2192H (https://ui.adsabs.harvard.edu/abs/1999PNAS...96.2192H).
doi:10.1073/pnas.96.5.2192 (https://doi.org/10.1073%2Fpnas.96.5.2192). PMC 26759 (http
s://www.ncbi.nlm.nih.gov/pmc/articles/PMC26759). PMID 10051617 (https://pubmed.ncbi.nl
m.nih.gov/10051617).
Kitano H (March 2002). "Systems biology: a brief overview". Science. 295 (5560): 1662–
1664. Bibcode:2002Sci...295.1662K (https://ui.adsabs.harvard.edu/abs/2002Sci...295.1662
K). doi:10.1126/science.1069492 (https://doi.org/10.1126%2Fscience.1069492).
PMID 11872829 (https://pubmed.ncbi.nlm.nih.gov/11872829). S2CID 2703843 (https://api.se
manticscholar.org/CorpusID:2703843).
Ptashne, M. "A Genetic Switch: Phage Lambda Revisited", 3rd edition 2003
Ptashne M (June 2005). "Regulation of transcription: from lambda to eukaryotes" (https://doi.
org/10.1016%2Fj.tibs.2005.04.003). Trends in Biochemical Sciences. 30 (6): 275–279.
doi:10.1016/j.tibs.2005.04.003 (https://doi.org/10.1016%2Fj.tibs.2005.04.003).
PMID 15950866 (https://pubmed.ncbi.nlm.nih.gov/15950866).
Snyder L, Champness W (2007). Molecular Genetics of Bacteria (3rd ed.). (Contains an
informative and well illustrated overview of bacteriophage lambda)
"Bacteriophage Lambda Infection" (https://web.archive.org/web/20140319191609/http://spla
sho.com/blog/essays/bacteriophage-lambda/). Splasho. Archived from the original (http://spl
asho.com/blog/essays/bacteriophage-lambda/) on 19 March 2014. (illustrates genes active
at all stages in lifecycle)

External links
Life Cycle, Basic Animation of Lambda Lifecyecle (http://www.blackwellpublishing.com/wagn
er/animations/lambdaw/lambdaw.html) (illustrates infection and lytic/lysogenic pathways with
some protein and transcription detail)
Time-lapse microscopy video (https://www.youtube.com/watch?v=sLkZ9FPHJGM) from MIT
showing both lysis and lysogeny by phage lambda
Lambda Phage Life cycle (https://www.youtube.com/watch?v=_vR-J05mHhQ) (basic visual
demonstration of Lambda bacteriophage life cycle)
Lambda Phage genome in GenBank (https://www.ncbi.nlm.nih.gov/nuccore/9626243?report
=genbank)
Lambda Phage Reference Proteome from UniProt (https://www.uniprot.org/uniprot/?query=or
ganism:10710+keyword:1185)
Lambda Phage Protein Structures in NCBI (https://www.ncbi.nlm.nih.gov/structure/?term=txid
10710) (3D display of protein structures for bacteriophage Lambda)

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