3.4.21.88: Repressor LexA
This is an abbreviated version!
For detailed information about Repressor LexA, go to the full flat file.
Word Map on EC 3.4.21.88
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3.4.21.88
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reca
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lambda
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phage
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single-stranded
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regulon
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umud
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prophage
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mitomycin
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dna-damaging
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damage-inducible
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colicins
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sos-induced
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coprotease
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uv-irradiated
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nalidixic
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autodigestion
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self-cleavage
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sula
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lexa-binding
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reca430
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lysogens
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reca-dependent
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lexa-regulated
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reca-mediated
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lexadef
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promoter-operator
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drug development
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translesion
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antirepressors
- 3.4.21.88
- reca
- lambda
- phage
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single-stranded
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regulon
- umud
- prophage
- mitomycin
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dna-damaging
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damage-inducible
- colicins
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sos-induced
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coprotease
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uv-irradiated
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nalidixic
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autodigestion
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self-cleavage
- sula
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lexa-binding
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reca430
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lysogens
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reca-dependent
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lexa-regulated
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reca-mediated
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lexadef
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promoter-operator
- drug development
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translesion
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antirepressors
Reaction
Hydrolysis of Ala84-/-Gly bond in repressor LexA =
Synonyms
Cg2114, LexA, LexA protein, LexA repressor, LexA transcriptional repressor, LexA1, lexA_1, MtLexA, SOS regulatory protein dinR
ECTree
3.4.21.88 Repressor LexAAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.21.88 - Repressor LexA
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DNA + H2O
LexA-DNA complexes
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detected by electrophoretical mobility shift assays, LexA repressor is the key regulatory protein of the DNA repair system, the SOS response. LexA is directly involved in SOS induction of the Staphylococcus aureus pathogenicity islands, SaPIs. LexA represses SaPI operon I containing ORF5, ORF7, 8 and 9
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Repressor LexA + H2O
LexA cleavage products
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intermolecular cleavage reaction in which the C-terminal fragment of LexA acts as an enzyme to cleave other molecules of LexA
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Repressor LexA + H2O
LexA cleavage products
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Ser-119 is a nucleophile and Lys-156 is an activator
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additional information
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repressor LexA exhibits a RecA-independent and alkaline pH-dependent autoproteolytic cleavage. The autoproteolytic cleavage occurs at pH 8.5 and above, is stimulated by the addition of Ca2+ and in the temperature range of 3057°C. The cleavage occurs at the peptide bond between Ala84 and Gly85, and optimal cleavage requires the presence of Ser118and Lys159. Cleavage of Anabaena LexA is affected upon deletion of three amino acids, G86L87I88
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additional information
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repressor LexA exhibits a RecA-independent and alkaline pH-dependent autoproteolytic cleavage. The autoproteolytic cleavage occurs at pH 8.5 and above, is stimulated by the addition of Ca2+ and in the temperature range of 3057°C. The cleavage occurs at the peptide bond between Ala84 and Gly85, and optimal cleavage requires the presence of Ser118and Lys159. Cleavage of Anabaena LexA is affected upon deletion of three amino acids, G86L87I88
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additional information
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repressor LexA exhibits a RecA-independent and alkaline pH-dependent autoproteolytic cleavage. The autoproteolytic cleavage occurs at pH 8.5 and above, is stimulated by the addition of Ca2+ and in the temperature range of 3057°C. The cleavage occurs at the peptide bond between Ala84 and Gly85, and optimal cleavage requires the presence of Ser118and Lys159. Cleavage of Anabaena LexA is affected upon deletion of three amino acids, G86L87I88
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additional information
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LexA binds to dinBox1 and to half-site dinBox1b in the SOS boxes in the lysogenic promoter P1 of phage GIL01. The dinBox1 is a 14-bp long sequence in the P1 promoter region that is similar to the consensus LexA binding site in Bacillus subtilis (CGAAC(n)4GTTCG). Transcription from promoter P1 is regulated by host LexA and phage-borne factors
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additional information
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LexA binds to dinBox1 and to half-site dinBox1b in the SOS boxes in the lysogenic promoter P1 of phage GIL01. The dinBox1 is a 14-bp long sequence in the P1 promoter region that is similar to the consensus LexA binding site in Bacillus subtilis (CGAAC(n)4GTTCG). Transcription from promoter P1 is regulated by host LexA and phage-borne factors
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additional information
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LexA paralogue can activate transcription
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additional information
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C-terminal fragment of lambda repressor cleaves the LexA substrate about as efficiently as does the lexA enzyme
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inhibits gene activation by the AraC protein
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additional information
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RecA protein and single-stranded DNA are required for activity being attributed to a Ser/Lys dyad. The LexA protein represses the SOS regulon, which regulates the genes involved in DNA repair. In the presence of single-stranded DNA, the RecA protein interacts with repressor LexA, causing it to undergo an autocatalytic cleavage which disrupts the DNA-binding part of the repressor, and inactivates it. The consequent derepression of the SOS regulon leads to DNA repair
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additional information
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LexA repressor coordinately controls about 20 unlinked genes comprising the bacterial SOS response, an inducible DNA repair system, these genes are necessary for functions as diverse as mutagenesis, DNA repair, recombionation, cell division, and prophage induction, SOS response is activated upon autoproteolysis of LexA repressor into its two separate domains
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additional information
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LexA repressor coordinately controls about 20 unlinked genes comprising the bacterial SOS response, an inducible DNA repair system, these genes are necessary for functions as diverse as mutagenesis, DNA repair, recombionation, cell division, and prophage induction, SOS response is activated upon autoproteolysis of LexA repressor into its two separate domains
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additional information
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interaction of enzyme with DNA motifs recA and yebG. Dissociation rate is 0.045 per s for recA and 0.13 per s for yebG with short-ranged binding potentials showing a stiff hydrogen-bonding network between protein and DNA
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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intact LexA dimerises by the carboxyterminal domain, and binds to DNA sequences via a helix-turn-helix in its amino-terminal domain. Upon self-cleavage between residues Ala84 and Gly85, LexA dissociates from its DNA targets (SOS boxes), causing the induction of the SOS regulon. Two distinct conformations of the LexA cleavage site region
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additional information
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RecA stimulates self-cleavage of a scissile peptide bond between Ala84 and Gly85, thereby de-activating LexA. RecA cannot induce self-cleavage in LexA that is bound to target DNA operator sites. In unbound LexA, the DNA-binding domains sample different conformations. One of these conformations is captured when LexA is bound to operator targets and this precludes interaction by RecA. Hence, the conformational flexibility of unbound LexA is the key element in establishing a co-ordinated SOS response. While LexA exhibits diverse dissociation rates from operators, it interacts extremely rapidly with DNA target sites. Modulation of LexA activity changes the occurrence of persister cells in bacterial populations
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additional information
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genome-wide mapping of LexA1 binding sites using ChIP-qPCR, determination of genes directly associated with LexA1 binding sites, overview. the LexA1 binding site is a 16 nt palindrome whose consensus is roughly CTnnACnnnnGTnnAG, it is present in all sequences shown to bind to LexA1 in serovar Copenhageni. Almost every peak of LexA1 binding is located upstream of a gene, in potential regulatory regions. LexA1-bound genes show decreased or no differential expression after DNA damage
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additional information
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genome-wide mapping of LexA1 binding sites using ChIP-qPCR, determination of genes directly associated with LexA1 binding sites, overview. the LexA1 binding site is a 16 nt palindrome whose consensus is roughly CTnnACnnnnGTnnAG, it is present in all sequences shown to bind to LexA1 in serovar Copenhageni. Almost every peak of LexA1 binding is located upstream of a gene, in potential regulatory regions. LexA1-bound genes show decreased or no differential expression after DNA damage
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additional information
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presence of LexA-Myc is present in cell-free extract from Mycobacterium tuberculosis expressing pKS04 but not pKS04mut1 or pEJMyc. The translational start site for LexA is upstream of residue 1, it is translated from a start codon 57 bp further upstream at the transcriptional start site
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additional information
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qualitative analysis of DNA-binding activities of MtLexA and its mutants, MtLexA binds to dsDNA with the consensus sequence GAAC-N4-GTTT/C. Modeling of the MtLexA-DNA complex, overview. The length of the flanking sequences of bound DNA does not affect DNA binding by LexA. Analysis of autocatalytic cleavage of MtLexA and enzyme mutants
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additional information
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qualitative analysis of DNA-binding activities of MtLexA and its mutants, MtLexA binds to dsDNA with the consensus sequence GAAC-N4-GTTT/C. Modeling of the MtLexA-DNA complex, overview. The length of the flanking sequences of bound DNA does not affect DNA binding by LexA. Analysis of autocatalytic cleavage of MtLexA and enzyme mutants
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additional information
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presence of LexA-Myc is present in cell-free extract from Mycobacterium tuberculosis expressing pKS04 but not pKS04mut1 or pEJMyc. The translational start site for LexA is upstream of residue 1, it is translated from a start codon 57 bp further upstream at the transcriptional start site
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additional information
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qualitative analysis of DNA-binding activities of MtLexA and its mutants, MtLexA binds to dsDNA with the consensus sequence GAAC-N4-GTTT/C. Modeling of the MtLexA-DNA complex, overview. The length of the flanking sequences of bound DNA does not affect DNA binding by LexA. Analysis of autocatalytic cleavage of MtLexA and enzyme mutants
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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Rhodobacter capsulatus LexA binds to the predicted promoter regions of lexA, recA, and cckA and represses cckA and recA transcription. Putative LexA binding sites are present 5' of SOS response gene homologues and the RcGTA regulatory gene cckA
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additional information
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Rhodobacter capsulatus LexA binds to the predicted promoter regions of lexA, recA, and cckA and represses cckA and recA transcription. Putative LexA binding sites are present 5' of SOS response gene homologues and the RcGTA regulatory gene cckA
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additional information
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Rhodobacter capsulatus LexA binds to the predicted promoter regions of lexA, recA, and cckA and represses cckA and recA transcription. Putative LexA binding sites are present 5' of SOS response gene homologues and the RcGTA regulatory gene cckA
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additional information
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Rhodobacter capsulatus LexA binds to the predicted promoter regions of lexA, recA, and cckA and represses cckA and recA transcription. Putative LexA binding sites are present 5' of SOS response gene homologues and the RcGTA regulatory gene cckA
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additional information
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Rhodobacter capsulatus LexA binds to the predicted promoter regions of lexA, recA, and cckA and represses cckA and recA transcription. Putative LexA binding sites are present 5' of SOS response gene homologues and the RcGTA regulatory gene cckA
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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involved in SOS response to DNA damage through recA-lexA regulon
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LexA is a DNA-binding protein
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LexA is a DNA-binding protein
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LexA is a DNA-binding protein
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LexA interacts with its own promoter. LexA-orthologue binds as a dimer to 12 bp direct repeats containing a CTA-N9-CTA sequence conserved in two target genes, lexA and crhR. Recombinant LexA does not bind the crhR transcript, it binds non-specifically to RNA and consequently does not appear to exert its effect on gene expression at the post-transcriptional level. Recombinant LexA binds the crhR gene as a dimer
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LexA paralogue can activate transcription
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upon binding to aryl hydrocarbon receptor ligands, XDVs (recombinant aryl hydrocarbon receptors) act as functional transcription factors, independent of aryl hydrocarbon receptor nuclear translocator, to induce the expression of a reporter gene (LacZ) driven by a synthetic LexA-responsive promoter in the yeast strain L40
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LexA binds a 14 bp palindromic motif with consensus sequence TGTTC-N4-GAACA, computational analysis of the recognition motif, comparative genomics analysis. The Verrucomicrobia LexA protein targets tandem binding sites in LexA promoters
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Vibrio cholerae LexA coordinates CTX prophage gene expression, overview. CTXPhi genes require for virion production initiate transcription from the strong PA promoter, which is dually repressed in lysogens by the phage-encoded repressor RstR and the host-encoded SOS repressor LexA. RstR both positively and negatively autoregulates its own expression from this promoter. LexA is absolutely required for RstR-mediated activation of PR transcription. Mechanisms, detailed overview
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LexA-gp7 interaction forms a heterohexamer with 2:4 stoichiometry. Gp7 interacts with Bacillus thuringiensis LexA C-terminal domain
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LexA-gp7 interaction forms a heterohexamer with 2:4 stoichiometry. Gp7 interacts with Bacillus thuringiensis LexA C-terminal domain
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