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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 designated Std (stop transfer defective). In this study, we examined the effects of overproduction of some molecular...

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Identifiers

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

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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.

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

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

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

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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 ↗

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