Two modes of binding of DinI to RecA filament provide a new insight into the regulation of SOS response by DinI protein.

ABSTRACT: RecA protein plays a principal role in bacterial SOS response to DNA damage. The induction of the SOS response is well understood and involves the cleavage of the LexA repressor catalyzed by the RecA nucleoprotein filament. In contrast, our understanding of the regulation and termination of the SOS response is much more limited. RecX and DinI are two major regulators of RecA's ability to promote LexA cleavage and strand exchange reaction, and are believed to modulate its activity in ongoing SOS events. DinI's function in the SOS response remains controversial, since its interaction with the RecA filament is concentration dependent and may result in either stabilization or depolymerization of the filament. The 17 C-terminal residues of RecA modulate the interaction between DinI and RecA. We

SUBMITTER: Galkin VE 

PROVIDER: S-EPMC3089025 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature