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Article

Two SecG molecules present in a single protein translocation machinery are functional even after crosslinking.

Journal of biochemistry - 1 Jul 2000

Nagamori S, Nishiyama K, Tokuda H

Abstract excerpt

SecG, a membrane component of the protein translocation apparatus of Escherichia coli, undergoes membrane topology inversion, which is coupled to the membrane insertion and deinsertion cycle of SecA. Eighteen SecG derivatives possessing a single cysteine residue at various positions were construc...

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Identifiers

PMID: 10876167
DOI: 10.1093/oxfordjournals.jbchem.a022723

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-10876167-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

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Two SecG molecules present in a single protein translocation machinery are functional even after crosslinking.PMID 10876167Read ↗

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

Glycolipozyme MPIase is essential for topology inversion of SecG during preprotein translocation.Semantic proximity Read ↗

Nearest neighbor analysis of the SecYEG complex. 1. Identification of a SecY-SecG interface.Semantic proximity Read ↗

SecY-SecY and SecY-SecG contacts revealed by site-specific crosslinking.Semantic proximity Read ↗

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

Depletion of SecDF-YajC causes a decrease in the level of SecG: implication for their functional interaction.Semantic proximity Read ↗

Multiple SecA molecules drive protein translocation across a single translocon with SecG inversion.Semantic proximity Read ↗

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

In vivo membrane topology of Escherichia coli SecA ATPase reveals extensive periplasmic exposure of multiple functionally important domains clustering on one face of SecA.Semantic proximity Read ↗

Roles of SecG in ATP- and SecA-dependent protein translocation.Semantic proximity Read ↗

Cross-linked SecA dimers are not functional in protein translocation.Semantic proximity Read ↗

Mapping an interface of SecY (PrlA) and SecE (PrlG) by using synthetic phenotypes and in vivo cross-linking.Semantic proximity Read ↗

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