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Article

Overproduction of SecA suppresses the export defect caused by a mutation in the gene encoding the Escherichia coli export chaperone secB.

Journal of bacteriology - 1 May 1999

Cook H A, Kumamoto C A

Abstract excerpt

SecB is a cytosolic protein required for rapid and efficient export of particular periplasmic and outer membrane proteins in Escherichia coli. SecB promotes export by stabilizing newly synthesized precursor proteins in a nonnative conformation and by targeting the precursors to the inner membrane. Biochemical studies suggest that SecB facilitates precursor targeting by binding to the SecA protein, a component of...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 10322000
DOI: 10.1128/JB.181.10.3010-3017.1999
PMCID: PMC93754

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

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Overproduction of SecA suppresses the export defect caused by a mutation in the gene encoding the Escherichia coli export chaperone secB.PMID 10322000Read ↗

A mutation of Escherichia coli SecA protein that partially compensates for the absence of SecB.Semantic proximity Read ↗

Mutations of the molecular chaperone protein SecB which alter the interaction between SecB and maltose-binding protein.Semantic proximity Read ↗

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Isolation and analysis of dominant secA mutations in Escherichia coli.Semantic proximity Read ↗

Defining the role of the Escherichia coli chaperone SecB using comparative proteomics.Semantic proximity Read ↗

Both transmembrane domains of SecG contribute to signal sequence recognition by the Escherichia coli protein export machinery.Semantic proximity Read ↗

SecY variants that interfere with Escherichia coli protein export in the presence of normal secY.Semantic proximity Read ↗

Complexes between protein export chaperone SecB and SecA. Evidence for separate sites on SecA providing binding energy and regulatory interactions.Semantic proximity Read ↗

A new genetic selection identifies essential residues in SecG, a component of the Escherichia coli protein export machinery.Semantic proximity Read ↗

Dimeric SecA is essential for protein translocation.Semantic proximity Read ↗

Recognition of secretory proteins in Escherichia coli requires signals in addition to the signal sequence and slow folding.Semantic proximity Read ↗

SecA interacts with ribosomes in order to facilitate posttranslational translocation in bacteria.Semantic proximity Read ↗

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