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Cited by 417

The DOI matches its Crossref record; 212 of the 212 references it cites were found in a registry or an index.

Regulation of Bacterial RecA Protein Function

Cox, Michael M.·2007·Critical Reviews in Biochemistry and Molecular Biology

Abstract

The RecA protein is a recombinase functioning in recombinational DNA repair in bacteria. RecA is regulated at many levels. The expression of the recA gene is regulated within the SOS response. The activity of the RecA protein itself is autoregulated by its own C-terminus. RecA is also regulated by the action of other proteins. To date, these include the RecF, RecO, RecR, DinI, RecX, RdgC, PsiB, and UvrD proteins. The SSB protein also indirectly affects RecA function by competing for ssDNA binding sites. The RecO and RecR, and possibly the RecF proteins, all facilitate RecA loading onto SSB-coated ssDNA. The RecX protein blocks RecA filament extension, and may have other effects on RecA activity. The DinI protein stabilizes RecA filaments. The RdgC protein binds to dsDNA and blocks RecA access to dsDNA. The PsiB protein, encoded by F plasmids, is uncharacterized, but may inhibit RecA in some manner. The UvrD helicase removes RecA filaments from RecA. All of these proteins function in a network that determines where and how RecA functions. Additional regulatory proteins may remain to be discovered. The elaborate regulatory pattern is likely to be reprised for RecA homologues in archaeans and eukaryotes.

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Metadata

Authors
Cox, M. M.
Venue
Critical Reviews in Biochemistry and Molecular Biology
Published
2007-01
Volume
42
Issue
1
Pages
41-63
ISSN
  • 0045-6411 (ISSN-L)
  • 1040-9238
  • 1549-7798
OpenAlex
W2084802036
Cited by
417
References
212
FWCI
1.32
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Regulation of Bacterial RecA Protein Function. https://app.cochat.ai/papers/10.1080/10409230701260258
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Cox, M. M. (2007). Regulation of Bacterial RecA Protein Function. Critical Reviews in Biochemistry and Molecular Biology. https://doi.org/10.1080/10409230701260258

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