Results 11 to 20 of about 4,885 (120)

Conservation of the LexA repressor binding site in Deinococcus radiodurans

Journal of Integrative Bioinformatics, 2008
The LexA protein is a transcriptional repressor of the bacterial SOS DNA repair system, which comprises a set of DNA repair and cellular survival genes that are induced in response to DNA damage.
Khan Feroz, Singh S. P., Mishra B. N.
doaj   +2 more sources

Reductions in bacterial viability stimulate the production of Extra-intestinal Pathogenic Escherichia coli (ExPEC) cytoplasm-carrying Extracellular Vesicles (EVs).

PLoS Pathogens, 2022
Extra-intestinal Pathogenic Escherichia coli (ExPEC) is defined as an extra-intestinal foodborne pathogen, and several dominant sequence types (STs) ExPEC isolates are highly virulent, with zoonotic potential.
Min Jiang, Zhongxing Wang, Fufang Xia, Zhe Wen, Rui Chen, Dongyu Zhu, Min Wang, Xiangkai Zhuge, Jianjun Dai   +8 more
doaj   +1 more source

A DNA damage-induced, SOS-independent checkpoint regulates cell division in Caulobacter crescentus. [PDF]

PLoS Biology, 2014
Cells must coordinate DNA replication with cell division, especially during episodes of DNA damage. The paradigm for cell division control following DNA damage in bacteria involves the SOS response where cleavage of the transcriptional repressor LexA ...
Joshua W Modell, Tracy K Kambara, Barrett S Perchuk, Michael T Laub   +3 more
doaj   +1 more source

Biochemical characterization of Borrelia burgdorferi's RecA protein. [PDF]

PLoS ONE, 2017
RecA plays key roles in DNA recombination, replication and repair. Mutation of recA in the Lyme disease spirochete, Borrelia burgdorferi, fails to produce some of the phenotypes expected from study of recA mutation in other organisms.
Shu Hui Huang, Madison A Hart, Matthew Wade, McKayla R Cozart, Siobhan L McGrath, Kerri Kobryn   +5 more
doaj   +1 more source

In vitro study of the interaction of the LexA represser and the UvrC protein with a uvrC regulatory region [PDF]

FEBS Letters, 1986
The in vitro interaction of the LexA repressor with a regulatory region of the uvrC gene has been studied by polyacrylamide gel electrophoresis. Although the uvrC promoter region shows some homology with the canonic LexA binding site, no specific binding of the repressor to this DNA sequence could be observed, but only a cooperative nonspecific binding.
Granger-Schnarr, Michéle, Schnarr, Manfred, van Sluis, Cees A.   +2 more
openaire   +2 more sources

RNA-seq profiling reveals novel target genes of LexA in the cyanobacterium Synechocystis sp. PCC 6803

Frontiers in Microbiology, 2016
LexA is a well-established transcriptional repressor of SOS genes induced by DNA damage in E. coli and other bacterial species. However, LexA in the cyanobacterium Synechocystis sp. PCC 6803 has been suggested not to be involved in SOS response.
Ayumi eKizawa, Akihito eKawahara, Yasushi eTakimura, Yoshitaka eNishiyama, Yukako eHihara, Yukako eHihara   +5 more
doaj   +1 more source

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
Y, Ebina, Y, Takahara, F, Kishi, A, Nakazawa, R, Brent   +4 more
openaire   +2 more sources

The amino-terminal domain of LexA repressor is alpha-helical but differs from canonical helix-turn-helix proteins: a two-dimensional 1H NMR study. [PDF]

Proceedings of the National Academy of Sciences, 1989
The amino-terminal DNA binding domain of LexA repressor consisting of 84 amino acid residues has been studied by two-dimensional 1H NMR. Sequence-specific 1H resonance assignments were made for the first 60 amino acid residues. The secondary structure of this part of the protein contains three alpha-helices in the peptide segments 8-20, 28-35, and 41 ...
Lamerichs, R. M. J. N., Padilla, A., Boelens, R., Kaptein, R., Ottleben, G., Ruterjans, H., Granger-Schnarr, M., Oertel, P., Schnarr, M.   +8 more
openaire   +3 more sources

The Verrucomicrobia LexA-binding Motif: Insights into the Evolutionary Dynamics of the SOS Response

Frontiers in Molecular Biosciences, 2016
The SOS response is the primary bacterial mechanism to address DNA damage, coordinating multiple cellular processes that include DNA repair, cell division and translesion synthesis.
Ivan Erill, Susana Campoy, Sefa Kılıç, Jordi Barbé   +3 more
doaj   +1 more source

Design and comparative characterization of RecA variants

Scientific Reports, 2021
RecA plays a central role in DNA repair and is a main actor involved in recombination and activation of the SOS response. It is also used in the context of biotechnological applications in recombinase polymerase isothermal amplification (RPA).
Elsa del Val, William Nasser, Hafid Abaibou, Sylvie Reverchon   +3 more
doaj   +1 more source