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Article

Suppression of ftsH mutant phenotypes by overproduction of molecular chaperones.

Journal of bacteriology - 1 Feb 1996

Shirai Y, Akiyama Y, Ito K

Abstract excerpt

Decreased intracellular levels of FtsH, a membrane-bound ATPase, led to retardation of growth and protein export, as well as to an abnormal translocation of alkaline phosphatase that had been attached to a cytoplasmic domain of a multispanning membrane protein, SecY. The last phenotype is designa...

Topics

ATP-Dependent Proteases
Adenosine Triphosphatases
Alkaline Phosphatase
Bacterial Outer Membrane Proteins
Bacterial Proteins
Biological Transport
Chaperonin 10
Chaperonin 60
Escherichia coli
Escherichia coli Proteins
HSP90 Heat-Shock Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Membrane Proteins

Molecular Chaperones

Phenotype

SEC Translocation Channels

Suppression, Genetic

Source

Open in PubMed Open full text

Identifiers

PMID: 8576050
DOI: 10.1128/jb.178.4.1141-1145.1996
PMCID: PMC177777

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8576050-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Suppression of ftsH mutant phenotypes by overproduction of molecular chaperones.PMID 8576050Read ↗

Involvement of FtsH in protein assembly into and through the membrane. I. Mutations that reduce retention efficiency of a cytoplasmic reporter.Semantic proximity Read ↗

Involvement of FtsH in protein assembly into and through the membrane. II. Dominant mutations affecting FtsH functions.Semantic proximity Read ↗

FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins.Semantic proximity Read ↗

Degradation of SsrA-tagged proteins in streptococci.Semantic proximity Read ↗

DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli.Semantic proximity Read ↗

Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH).Semantic proximity Read ↗

Heat-shock proteins can substitute for SecB function during protein export in Escherichia coli.Semantic proximity Read ↗

The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits.Semantic proximity Read ↗

Suppression by enhanced RpoE activity of the temperature-sensitive phenotype of a degP ssrA double mutant in Escherichia coli.Semantic proximity Read ↗

Dislocation of membrane proteins in FtsH-mediated proteolysis.Semantic proximity Read ↗

Secretion and overproduction of carboxypeptidase Y by a Saccharomyces cerevisiae ssl1 mutant strain.Semantic proximity Read ↗

Superactive SecY variants that fulfill the essential translocation function with a reduced cellular quantity.Semantic proximity Read ↗

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