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Zusammenfassung: <jats:p>DinI is a recently described negative regulator of the SOS response in <jats:italic>Escherichia coli</jats:italic>. 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 α-helix in DinI as the active site of the protein. In an unusual example of molecular mimicry, a negatively charged surface on this α-helix, by imitating single-stranded DNA, interacts with the loop L2 homologous pairing region of RecA and interferes with the activation of RecA.</jats:p>
Umfang: 415-427
ISSN: 0890-9369
1549-5477
DOI: 10.1101/gad.862901