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Results 1 - 10 of 18 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.88evolution evolutionary dynamics of the SOS response involving the LexA enzyme, overview. The composition of the SOS genetic network and the binding motif of its transcriptional repressor, LexA, vary greatly across bacterial clades. Multiple sequence alignment of available LexA protein sequences for the phylum Verrucomicrobia, using the information in Escherichia coli LexA cyrstal structure (UniProt ID P0A7C2). The core Verrucomicrobia LexA regulon comprises three operons involved in DNA repair and mutagenesis, i.e. lexA, splB, and imuA-imuB-dnaE2. The Verrucomicrobia LexA regulon is highly variable and incorporates novel functions, overview 753691
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.88malfunction a lexA deletion strain WP3DELTAlexA shows no growth defects at 4-20°C -, 753674
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.88malfunction Bacillus thuringenis LexA binds to dinBox sequences in the temperate phage GIL01, repressing phage gene expression during lysogeny and providing the switch necessary to enter lytic development 717736
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.88malfunction deletion of the lexA gene results in the abolition of detectable RcGTA production and an about 10fold reduction in recipient capability. Expression of gene cckA, encoding the sensor kinase CckA, is increased over 5fold in the lexA mutant, and a lexA/cckA double mutant is found to have the same phenotype as a DELTAcckA single mutant in terms of RcGTA production. The RcGTA-deficient phenotype of the lexA mutant is largely due to the overexpression of cckA. RcGTA transposon Tn5 mutagenesis, overview -, 754015
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.88metabolism LexA-mediated repression of recA expression is a hallmark of the prototypical SOS response -, 754015
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.88more a complex of Mycobacterium tuberculosis LexA and the cognate SOS box is modeled in which the mutual orientation of the two N-terminal domains differs from that in the Escherichia coli LexA-DNA complex, complex structure analysis, overview -, 752390
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.88more a monodisperse mixture of gp7 and LexA appears as a 72-kDa heterohexameric complex composed of a tetrameric gp7 and dimeric LexA. Modeling of LexA-gp7 interaction in which gp7 acts as a small scaffold to orient the N-terminal and C-terminal domains of LexA such that the binding affinity to DNA is increased. LexA-gp7 Interaction forms a heterohexamer with 2:4 stoichiometry -, 755567
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.88more identification of putative Lex binding sites located 5' of typical SOS response coding sequences and also 5' of the RcGTA regulatory gene cckA, which encodes a hybrid histidine kinase homologue -, 754015
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.88physiological function isozyme LexA1 is probably the main regulator of the SOS response in Leptospira interrogans. In addition to both lexA genes and their operons, recA, recN and dinP are LexA1-bound and induced by DNA damage. LexA1 binds to the upstream sequence of both lexA1 and lexA2. Global transcriptional profiling during UV-C DNA damage response, overview. Two prophages heavily induce 12 h after UV-C irradiation involving LexA1 binding. Determination of LexA1 SOS box and DNA damage-inducible LexA1-bound genes -, 754925
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.88physiological function LexA is a central repressor in the SOS response. During infection of Bacillus thuringiensis with GIL01 bacteriophage, bacterial LexA represses the SOS response and the phage lytic cycle by binding DNA, the interaction is further stabilized upon binding of a viral protein, phage-borne gp7. Analysis of binding stoichiometry and potential interaction with LexA using surface plasmon resonance, static light scattering, and small-angle X-ray scattering, overview. LexA binds and represses expression through binding of dinBox1/1b, with LexA affinity for this region increased through interaction with a viral accessory protein gp7. Removal of the last six C-terminal residues of gp7 does not prevent its interaction with LexA. Modeling of LexA-gp7 interaction in which gp7 acts as a small scaffold to orient the N-terminal and C-terminal domains of LexA such that the binding affinity to DNA is increased. LexA-gp7 Interaction forms a heterohexamer with 2:4 stoichiometry. Under regular growth conditions, LexA binds SOS-box sequences upstream of DNA repair genes to suppress the expression of these genes -, 755567
Results 1 - 10 of 18 > >>