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Article

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

The Journal of biological chemistry - 25 Jan 1993

Gannon P M, Kumamoto C A

Abstract excerpt

SecB is a 16-kDa cytosolic chaperone protein that is required for efficient export of particular proteins in Escherichia coli. To identify regions of SecB that contribute to efficient protein export, we isolated secB point mutants that are defective for protein export in vivo. We obtained missense mutations at residues Leu75 (SecBL75Q), Cys76 (SecBC76Y), and Glu77 (SecBE77K) in the center of the secB gene. In...

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Identifiers

PMID: 8420934

Genes

MBP

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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.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutations of the molecular chaperone protein SecB which alter the interaction between SecB and maltose-binding protein.PMID 8420934Read ↗

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

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

A SecE mutation that modulates SecY-SecE translocase assembly, identified as a specific suppressor of SecY defects.Semantic proximity Read ↗

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

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

Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane.Semantic proximity Read ↗

Mutational analysis of transmembrane regions 3 and 4 of SecY, a central component of protein translocase.Semantic proximity Read ↗

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

Genetic analysis of SecY: additional export-defective mutations and factors affecting their phenotypes.Semantic proximity Read ↗

Protein translocation functions of Escherichia coli SecY: in vitro characterization of cold-sensitive secY mutants.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 cytoplasmic domain is important for the formation of a SecY-SecE translocator complex.Semantic proximity Read ↗

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