Article
Purification and biochemical characterization of Escherichia coli RecA proteins mutated in the putative DNA binding site.
The Journal of biological chemistry - 18 Mar 1994
Cazaux C, Larminat F, Villani G, Johnson N P, Schnarr M, Defais M
Abstract excerpt
Escherichia coli RecA protein plays a central role both in DNA repair and in recombination. We report biochemical properties of three new RecA proteins mutated at positions 199 (RecA694), 207 (RecA659), and 211 (RecA611) in the putative DNA binding site. RecA694 had a wild-type phenotype, whereas...
Topics
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Amino Acid Sequence
- Bacterial Proteins
- Base Sequence
- Binding Sites
- DNA Primers
- DNA, Single-Stranded
- DNA-Binding Proteins
- Escherichia coli
- Genes, Bacterial
- Kinetics
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Phenotype
- Rec A Recombinases
- Recombinant Proteins
- Serine Endopeptidases