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Article

Subunit dynamics in Escherichia coli preprotein translocase.

Proceedings of the National Academy of Sciences of the United States of America - 24 May 1994

Joly J C, Leonard M R, Wickner W T

Abstract excerpt

SecY, SecE, and band 1 copurify as the SecY/E integral membrane domain of Escherichia coli preprotein translocase. To measure the in vivo association of these polypeptides and assay possible exchange, plasmid-borne secY and secE genes were placed under control of the ara regulon and fused to DNA encoding the influenza hemagglutinin epitope. Cells were incubated with [35S]methionine, grown for a "chase" period,...

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Identifiers

PMID: 8197122
DOI: 10.1073/pnas.91.11.4703
PMCID: PMC43856

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Related research

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Research trail→

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Subunit dynamics in Escherichia coli preprotein translocase.PMID 8197122Read ↗

Bacterial protein translocation requires only one copy of the SecY complex in vivo.Semantic proximity Read ↗

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

Covalently dimerized SecA is functional in protein translocation.Semantic proximity Read ↗

Quaternary dynamics of the SecA motor drive translocase catalysis.Semantic proximity Read ↗

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

Interfering mutations provide in vivo evidence that Escherichia coli SecE functions in multimeric states.Semantic proximity Read ↗

Structure, function, and biogenesis of SecY, an integral membrane protein involved in protein export.Semantic proximity Read ↗

Two-stage binding of SecA to the bacterial translocon regulates ribosome-translocon interaction.Semantic proximity Read ↗

Additional in vitro and in vivo evidence for SecA functioning as dimers in the membrane: dissociation into monomers is not essential for protein translocation in Escherichia coli.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 ↗

SecG is an auxiliary component of the protein export apparatus of Escherichia coli.Semantic proximity Read ↗

A cytoplasmic domain is important for the formation of a SecY-SecE translocator complex.Semantic proximity Read ↗

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