Literature DB >> 1538397

Genetical and biochemical evidence for the involvement of the coprotease domain of Escherichia coli RecA protein in recombination.

C Cazaux1, M Defais.   

Abstract

RecA amino acid residue 204 is involved in the coprotease domain of the protein responsible for the induction of mutagenic repair. Two mutations were created at this site leading to the addition of either a methyl or an isopropyl group on the original glycine. Analyses of both the in vivo and the in vitro properties of these mutated proteins demonstrated that this residue 204 is involved in many RecA activities, suggesting that this site could allosterically direct conformational changes in the protein or could be situated in a region interacting with many RecA cofactors.

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Year:  1992        PMID: 1538397     DOI: 10.1016/0022-2836(92)90243-d

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  2 in total

1.  New mutations in and around the L2 disordered loop of the RecA protein modulate recombination and/or coprotease activity.

Authors:  F Larminat; C Cazaux; M Germanier; M Defais
Journal:  J Bacteriol       Date:  1992-10       Impact factor: 3.490

2.  Inducibility of the SOS response in a recA730 or recA441 strain is restored by transformation with a new recA allele.

Authors:  C Cazaux; A M Mazard; M Defais
Journal:  Mol Gen Genet       Date:  1993-08
  2 in total

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