Alteration of lysine 178 in the hinge region of the Escherichia coli ada protein interferes with activation of ada, but not alkA, transcription.

doi:10.1128/jb.177.5.1268-1274.1995

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Article

Alteration of lysine 178 in the hinge region of the Escherichia coli ada protein interferes with activation of ada, but not alkA, transcription.

Journal of bacteriology - 1 Mar 1995

Saget B M, Shevell D E, Walker G C

Abstract excerpt

The ada gene of Escherichia coli K-12 encodes the 39-kDa Ada protein, which consists of two domains joined by a hinge region that is sensitive to proteolytic cleavage in vitro. The amino-terminal domain has a DNA methyltransferase activity that repairs the S-diastereoisomer of methylphosphotriesters while the carboxyl-terminal domain has a DNA methyltransferase activity that repairs O6-methylguanine and...

Topics

Adaptation, Physiological
Bacterial Proteins
Base Sequence
DNA Glycosylases
DNA Repair
Enzyme Activation
Escherichia coli
Escherichia coli Proteins
Gene Expression Regulation, Bacterial
Lysine
Methyltransferases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Multienzyme Complexes

Mutation

N-Glycosyl Hydrolases

O(6)-Methylguanine-DNA Methyltransferase

Structure-Activity Relationship

Transcription Factors

Source

Open in PubMed Open full text

Identifiers

PMID: 7868601
DOI: 10.1128/jb.177.5.1268-1274.1995
PMCID: PMC176733

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7868601-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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