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• W2988780623 endingPage "105642" @default.
• W2988780623 startingPage "105642" @default.
• W2988780623 abstract "The recombinases present in the all kingdoms in nature play a crucial role in DNA metabolism processes such as replication, repair, recombination and transcription. However, till date, the role of RecA in the deadly foodborne pathogen Listeria monocytogenes remains unknown. In this study, the authors show that L. monocytogenes expresses recA more than two-fold in vivo upon exposure to the DNA damaging agents, methyl methanesulfonate and ultraviolet radiation. The purified L. monocytogenes RecA protein show robust binding to single stranded DNA. The RecA is capable of forming displacement loop and hydrolyzes ATP, whereas the mutant LmRecAK70A fails to hydrolyze ATP, showing conserved walker A and B motifs. Interestingly, L. monocytogenes RecA and LmRecAK70A perform the DNA strand transfer activity, which is the hallmark feature of RecA protein with an oligonucleotide-based substrate. Notably, L. monocytogenes RecA readily cleaves L. monocytogenes LexA, the SOS regulon and protects the presynaptic filament from the exonuclease I activity. Altogether, this study provides the first detailed characterization of L. monocytogenes RecA and presents important insights into the process of homologous recombination in the gram-positive foodborne bacteria L. monocytogenes." @default.
• W2988780623 created "2019-11-22" @default.
• W2988780623 creator A5051896421 @default.
• W2988780623 creator A5086373815 @default.
• W2988780623 date "2020-02-01" @default.
• W2988780623 modified "2023-09-24" @default.
• W2988780623 title "Molecular and functional characterization of the Listeria monocytogenes RecA protein: Insights into the homologous recombination process" @default.
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• W2988780623 doi "https://doi.org/10.1016/j.biocel.2019.105642" @default.
• W2988780623 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31698090" @default.
• W2988780623 hasPublicationYear "2020" @default.
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