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Article

Dimeric SecA is essential for protein translocation.

Proceedings of the National Academy of Sciences of the United States of America - 24 May 2005

Jilaveanu Lucia B, Zito Christopher R, Oliver Donald

Abstract excerpt

SecA facilitates bacterial protein translocation by its association with presecretory or membrane proteins and the SecYEG translocon channel. Once assembled, SecA ATPase undergoes cycles of membrane insertion and retraction at SecYEG that drive protein translocation in a stepwise fashion. SecA exists in equilibrium between a monomer and dimer, and association with its translocation ligands shifts this equilibrium...

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Identifiers

PMID: 15897468
DOI: 10.1073/pnas.0502774102
PMCID: PMC1140455

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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

Dimeric SecA is essential for protein translocation.PMID 15897468Read ↗

Reexamination of the role of the amino terminus of SecA in promoting its dimerization and functional state.Semantic proximity Read ↗

Covalently dimerized SecA is functional in protein translocation.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 ↗

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

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

SecY and SecA interact to allow SecA insertion and protein translocation across the Escherichia coli plasma membrane.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 ↗

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

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

Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA.Semantic proximity Read ↗

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