A Model for the Abrogation of the SOS Response by an SOS Protein: a Negatively Charged Helix in DinI Mimics DNA in Its Interaction with RecA

Overview

Journal Genes Dev

Specialty Molecular Biology

Date 2001 Mar 7

PMID 11230150

Citations 25

Authors

O N Voloshin

B. E. Ramirez

A Bax

R D Camerini-Otero

Affiliations

Soon will be listed here.

Abstract

DinI is a recently described negative regulator of the SOS response in Escherichia coli. Here we show that it physically interacts with RecA and prevents the binding of single-stranded DNA to RecA, which is required for the activation of the latter. DinI also displaces ssDNA from a stable RecA-DNA cofilament, thus eliminating the SOS signal. In addition, DinI inhibits RecA-mediated homologous DNA pairing, but has no effect on actively proceeding strand exchange. Biochemical data, together with the molecular structure, define the C-terminal alpha-helix in DinI as the active site of the protein. In an unusual example of molecular mimicry, a negatively charged surface on this alpha-helix, by imitating single-stranded DNA, interacts with the loop L2 homologous pairing region of RecA and interferes with the activation of RecA.

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