Reaction of LexA repressor with diisopropyl fluorophosphate. A test of the serine protease model.

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Article

Reaction of LexA repressor with diisopropyl fluorophosphate. A test of the serine protease model.

The Journal of biological chemistry - 5 Aug 1990

Roland K L, Little J W

Abstract excerpt

The LexA repressor of Escherichia coli modulates the expression of the SOS regulon. In the presence of DNA damaging agents in vivo, the 202-amino acid LexA repressor is inactivated by specific RecA-mediated cleavage of the Ala-84/Gly-85 peptide bond. In vitro. LexA cleavage requires activated RecA at neutral pH, and proceeds spontaneously at high pH in an intramolecular reaction termed autodigestion. A model has...

Topics

Amino Acid Sequence
Bacterial Proteins
Base Sequence
Chromatography, High Pressure Liquid
Cyanogen Bromide
Escherichia coli
Isoflurophate
Models, Biological
Molecular Sequence Data
Mutation
Oligonucleotide Probes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Peptide Fragments

Peptide Mapping

Protein Binding

Repressor Proteins

Serine Endopeptidases

Transcription Factors

Source

Open in PubMed

Identifiers

PMID: 2198279

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2198279-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Reaction of LexA repressor with diisopropyl fluorophosphate. A test of the serine protease model.PMID 2198279Read ↗

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