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Article

In vitro analysis of mutant LexA proteins with an increased rate of specific cleavage.

Journal of molecular biology - 20 Nov 1992

Roland K L, Smith M H, Rupley J A, Little J W

Abstract excerpt

Specific cleavage of LexA repressor plays a crucial role in the SOS response of Escherichia coli. In vivo, cleavage requires an activated form of RecA protein. However, previous work has shown that the mechanism of cleavage is unusual, in that the chemistry of cleavage is probably carried out by residues in the repressor, and not those in RecA; RecA appears to facilitate this reaction, acting as a coprotease. We...

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Identifiers

PMID: 1453451
DOI: 10.1016/0022-2836(92)90829-9

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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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In vitro analysis of mutant LexA proteins with an increased rate of specific cleavage.PMID 1453451Read ↗

Mutant LexA proteins with an increased rate of in vivo cleavage.Semantic proximity Read ↗

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Novel mechanism for UV sensitivity and apparent UV nonmutability of recA432 mutants: persistent LexA cleavage following SOS induction.Semantic proximity Read ↗

Analysis of recA mutants with altered SOS functions.Semantic proximity Read ↗

Reaction of LexA repressor with diisopropyl fluorophosphate. A test of the serine protease model.Semantic proximity Read ↗

Purification and biochemical characterization of Escherichia coli RecA proteins mutated in the putative DNA binding site.Semantic proximity Read ↗

Anti-mutagenic agent targeting LexA to combat antimicrobial resistance in mycobacteriaSemantic proximity Read ↗

Functional coupling of duplex translocation to DNA cleavage in a type I restriction enzyme.Semantic proximity Read ↗

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Disassembly of Escherichia coli RecA E38K/DeltaC17 nucleoprotein filaments is required to complete DNA strand exchange.Semantic proximity Read ↗

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