PMID:9605403
| Citation |
Bianco, PR and Weinstock, GM (1998) Characterization of RecA1332 in vivo and in vitro. A role for alpha-helix E as a liaison between the subunit-subunit interface and the DNA and ATP binding domains of RecA protein. Genes Cells 3:79-97 |
|---|---|
| Abstract |
The RecA protein of Escherichia coli is essential for homologous recombination and induction of the SOS response. RecA has three cysteines located at positions 90, 116 and 129. Chemical modification of these residues abolishes ATP hydrolysis and repressor cleavage, and causes a reduction in the DNA strand exchange and DNA strand annealing activities. Several mutants at each of these positions were isolated and partially characterized. One of these, recA1332, replaces cysteine 129 with methionine. Although this is a relatively conservative mutation based on hydrophobicity, recA1332 was completely defective for DNA repair but the purified protein was active for ATPase in vitro. |
| Links | |
| Keywords |
Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Binding Sites; Cations, Monovalent/pharmacology; Cysteine; DNA Repair; DNA, Bacterial/metabolism; DNA, Single-Stranded/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Models, Molecular; Mutagenesis; Mutation; Protein Structure, Secondary; Rec A Recombinases/chemistry; Rec A Recombinases/genetics; Rec A Recombinases/metabolism; Recombination, Genetic; SOS Response (Genetics) |
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