Genetical and biochemical evidence for the involvement of the coprotease domain of Escherichia coli RecA protein in recombination.
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.
Cazaux
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C
Laboratoire de Pharmacologie et de Toxicologie Fondamentales, C.N.R.S., Toulouse, France.
Defais
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M
D000255:Adenosine Triphosphate / Q000378:metabolism; D004252:DNA Mutational Analysis; D004260:DNA Repair; D004269:DNA, Bacterial / Q000235:genetics; D010450:Endopeptidases / Q000737:chemistry* / Q000378:metabolism; D006860:Hydrogen Bonding; D010641:Phenotype; D011938:Rec A Recombinases / Q000737:chemistry* / Q000378:metabolism; D011995:Recombination, Genetic; D013329:Structure-Activity Relationship
D004269:DNA, Bacterial; D000255:Adenosine Triphosphate; D011938:Rec A Recombinases; D010450:Endopeptidases