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PMID:11230150

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Citation

Voloshin, ON, Ramirez, BE, Bax, A and Camerini-Otero, RD (2001) 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. Genes Dev. 15:415-27

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.

Links

PubMed PMC312637 Online version:10.1101/gad.862901

Keywords

Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacterial Proteins/physiology; Base Sequence; DNA Primers; DNA, Bacterial/chemistry; DNA, Bacterial/metabolism; DNA, Bacterial/physiology; Escherichia coli Proteins; Molecular Mimicry; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Binding; Rec A Recombinases/metabolism; SOS Response (Genetics)

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ECOLI:DINI

enables

GO:0019899: enzyme binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P0A7G6

F

Seeded From UniProt

complete

See also

References

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