Inducibility of the SOS response in a recA730 or recA441 strain is restored by transformation with a new recA allele.
Escherichia coli RecA protein plays an essential role in both genetic recombination and SOS repair; in vitro RecA needs to bind ATP to promote both activities. Residue 264 is involved in this interaction; we have therefore created two new recA alleles, recA664 (Tyr264-->Glu) and recA665 (Tyr264-->His) bearing mutations at this site. As expected both mutations affected all RecA activities in vivo. Complementation experiments between these new alleles and wild-type recA or recA441 or recA730 alleles, both of which lead to constitutively activated RecA protein, were performed to further investigate the modulatory effects of these mutants on the regulation of SOS repair/recombination pathways. Our results provide further insight into the process of polymerization of RecA protein and its regulatory functions.
Cazaux
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C
Laboratoire de Pharmacologie et Toxicologie Fondamentales, CNRS UPR 8221, Toulouse, France.
Mazard
A M
AM
Defais
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M
D000483:Alleles; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics* / Q000254:growth & development; D005798:Genes, Bacterial; D005816:Genetic Complementation Test; D016297:Mutagenesis, Site-Directed; D017354:Point Mutation; D011938:Rec A Recombinases / Q000235:genetics*; D011995:Recombination, Genetic; D013014:SOS Response, Genetics; D014169:Transformation, Bacterial
D011938:Rec A Recombinases