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pro vyhledávání: '"Alison N. Grice"'
Autor:
Travis A Witkowski, Alison N Grice, DeAnna B Stinnett, Whitney K Wells, Megan A Peterson, Janelle M Hare
Publikováno v:
PLoS ONE, Vol 11, Iss 3, p e0152013 (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). Upon DNA damage, LexA cleaves itsel
Externí odkaz:
https://doaj.org/article/c2b965bcc84341cbb827e2e7d25270ff
Publikováno v:
Microbiology. 166:212-226
The DNA damage response of the multidrug-resistant pathogen Acinetobacter baumannii , which induces mutagenic UmuD′2C error-prone polymerases, differs from that of many bacteria. Acinetobacter species lack a LexA repressor, but induce gene transcri
Publikováno v:
PLoS ONE, Vol 9, Iss 4, p e93861 (2014)
The SOS response to DNA damage that induces up to 10% of the prokaryotic genome requires RecA action to relieve LexA transcriptional repression. In Acinetobacter species, which lack LexA, the error-prone polymerase accessory UmuDAb is instead require
Externí odkaz:
https://doaj.org/article/54dcb3577c96470c8f934f7fc8739afd
Publikováno v:
Microbiology
The DNA damage response of the multidrug-resistant pathogen Acinetobacter baumannii , which induces mutagenic UmuD′2C error-prone polymerases, differs from that of many bacteria. Acinetobacter species lack a LexA repressor, but induce gene transcri
Publikováno v:
PLoS ONE
PLoS ONE, Vol 9, Iss 4, p e93861 (2014)
PLoS ONE, Vol 9, Iss 4, p e93861 (2014)
The SOS response to DNA damage that induces up to 10% of the prokaryotic genome requires RecA action to relieve LexA transcriptional repression. In Acinetobacter species, which lack LexA, the error-prone polymerase accessory UmuDAb is instead require
Publikováno v:
FEMS microbiology letters. 334(1)
In the DNA damage response of most bacteria, UmuD forms part of the error-prone (UmuD′2)C polymerase V and is activated for this function by self-cleavage after DNA damage. However, the umuD homolog ( umuDAb ) present throughout the Acinetobacter g