Elucidating the Substrate Preference of the Bi-Functional Repressor-Protease LexA [PDF]
Biophysical Journal, 2013 The rise of drug resistance in bacteria is a growing problem, and poses a formidable medical and scientific challenge. Mutations - the driving force behind evolution and drug-resistance - have long been thought to arise spontaneously in bacteria, leading to the pessimistic view that the rise of drug resistance is inevitable. However, the acquisition of
Charlie Y. Mo
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LexA protein is a repressor of the colicin E1 gene.
Journal of Biological Chemistry, 1983 LexA protein is a repressor of several chromosomal genes involved in the SOS response in Escherichia coli. In previous experiments, we found that LexA protein may also be a repressor of the colicin E1 gene. We now present evidence that the purified LexA protein strongly repressed the in vitro transcription of the colicin E1 gene. As determined in DNase
Yasuhiko Ebina +4 more
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The carboxy‐terminal domain of the LexA repressor oligomerises essentially as the entire protein [PDF]
FEBS Letters, 1988 The ability of the isolated carboxy‐terminal domain of the LexA repressor of Escherichia coli to form dimers and tetramers has been investigated by equilibrium ultracentrifugation. This domain, that comprises the amino acids 85–202, is readily purified after self‐cleavage of the LexA repressor at alkaline pH.
Manfred Schnarr +3 more
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In Situ Single-Molecule Dynamics of the SOS-Repressor Lexa during Antibiotic Stress [PDF]
Biophysical Journal, 2020 Leonard Schärfen +3 more
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Purified lexA protein is a repressor of the recA and lexA genes. [PDF]
Proceedings of the National Academy of Sciences, 1981 Escherichia coli shows a pleiotropic response (the SOS response) to treatments that damage DNA or inhibit DNA replication. Previous evidence has suggested that the product of the lexA gene is involved in regulating the SOS response, perhaps as a repressor, and that it is sensitive to the recA protease.
John W. Little +2 more
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UmuDAb: An Error-Prone Polymerase Accessory Homolog Whose N-Terminal Domain Is Required for Repression of DNA Damage Inducible Gene Expression in Acinetobacter baylyi. [PDF]
PLoS ONE, 2016 In many bacteria, the DNA damage response induces genes (SOS genes) that were repressed by LexA. LexA represses transcription by binding to SOS promoters via a helix-turn-helix motif in its N-terminal domain (NTD).
Travis A Witkowski +5 more
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Structural Insights into Bacteriophage GIL01 gp7 Inhibition of Host LexA Repressor [PDF]
Structure, 2019 Bacteria identify and respond to DNA damage using the SOS response. LexA, a central repressor in the response, has been implicated in the regulation of lysogeny in various temperate bacteriophages. During infection of Bacillus thuringiensis with GIL01 bacteriophage, LexA represses the SOS response and the phage lytic cycle by binding DNA, an ...
Nathanael A. Caveney +8 more
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Non-equilibrium repressor binding kinetics link DNA damage dose to transcriptional timing within the SOS gene network. [PDF]
PLoS Genetics, 2018 Biochemical pathways are often genetically encoded as simple transcription regulation networks, where one transcription factor regulates the expression of multiple genes in a pathway.
Matthew J Culyba +4 more
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Integration of molecular modelling and in vitro studies to inhibit LexA proteolysis
Frontiers in Cellular and Infection Microbiology, 2023 IntroductionAs antibiotic resistance has become more prevalent, the social and economic impacts are increasingly pressing. Indeed, bacteria have developed the SOS response which facilitates the evolution of resistance under genotoxic stress.
Zachariah P. Schuurs +7 more
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The Escherichia coli LexA repressor-operator system works in mammalian cells. [PDF]
The EMBO Journal, 1988 We have demonstrated the use of the Escherichia coli LexA repressor-operator system to down-regulate gene expression in mouse cells. The LexA gene was placed downstream of the RSVLTR promoter with polyadenylation and splice signals from SV40. This expression unit was introduced into mouse Ltk- cells by calcium phosphate transfection and stable ...
Gary M. Smith +6 more
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