The role of transcriptional repressor activity of LexA in salt-stress responses of the cyanobacterium Synechocystis sp. PCC 6803 [PDF]
Scientific Reports, 2020 Different from typical LexA repressors in heterotrophic bacteria exerting SOS response by auto-cleavage, cyanobacterial LexAs, especially that of Synechocystis sp.
Kosuke Takashima +5 more
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Autodigestion of lexA and phage lambda repressors. [PDF]
Proceedings of the National Academy of Sciences, 1984 Proteolytic cleavage of lexA repressor is an early step in derepression of the SOS regulatory system of Escherichia coli. In vivo and in vitro data have indicated a role for recA protein in this specific proteolytic reaction. I show here that, under certain conditions, specific in vitro cleavage of highly-purified lexA protein can take place in the ...
John W. Little
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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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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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Bacteriophage crosstalk: coordination of prophage induction by trans-acting antirepressors. [PDF]
PLoS Genetics, 2011 Many species of bacteria harbor multiple prophages in their genomes. Prophages often carry genes that confer a selective advantage to the bacterium, typically during host colonization.
Sébastien Lemire +2 more
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Real-time kinetic studies of Mycobacterium tuberculosis LexA–DNA interaction
Bioscience Reports, 2021 Transcriptional repressor, LexA, regulates the ‘SOS’ response, an indispensable bacterial DNA damage repair machinery. Compared with its Escherichia coli ortholog, LexA from Mycobacterium tuberculosis (Mtb) possesses a unique N-terminal extension of ...
Chitral Chatterjee +4 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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Cells, 2021 Deinococcus bacteria are extremely resistant to radiation and able to repair a shattered genome in an essentially error-free manner after exposure to high doses of radiation or prolonged desiccation.
Laurence Blanchard, Arjan de Groot
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The LexA-RecA* structure reveals a lock-and-key mechanism for SOS activation
bioRxiv, 2023 The bacterial SOS response plays a key role in adaptation to DNA damage, including that caused by antibiotics. SOS induction begins when activated RecA*, an oligomeric nucleoprotein filament formed on single-stranded DNA, binds to and stimulates ...
Michael B. Cory +9 more
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Reaction of LexA repressor with diisopropyl fluorophosphate. A test of the serine protease model.
Journal of Biological Chemistry, 1990 The LexA repressor of Escherichia coli modulates the expression of the SOS regulon. In the presence of DNA damaging agents in vivo, the 202-amino acid LexA repressor is inactivated by specific RecA-mediated cleavage of the Ala-84/Gly-85 peptide bond. In vitro. LexA cleavage requires activated RecA at neutral pH, and proceeds spontaneously at high pH in
Kenneth L. Roland, John W. Little
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