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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 RecA611 and RecA659 were deficient in promoting both the self-cleavage of LexA repressor and the DNA-strand exchange...

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PMID: 8132549

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SSB

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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