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Article

Bacterial protein translocation requires only one copy of the SecY complex in vivo.

The Journal of cell biology - 3 Sept 2012

Park Eunyong, Rapoport Tom A

Abstract excerpt

The transport of proteins across the plasma membrane in bacteria requires a channel formed from the SecY complex, which cooperates with either a translating ribosome in cotranslational translocation or the SecA ATPase in post-translational translocation. Whether translocation requires oligomers of the SecY complex is an important but controversial issue: it determines channel size, how the permeation of small...

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Share to SecA Proteins
Share to Adenosine Triphosphatases
Share to Membrane Transport Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 22927464
DOI: 10.1083/jcb.201205140
PMCID: PMC3432775

Provenance

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

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

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Bacterial protein translocation requires only one copy of the SecY complex in vivo.PMID 22927464Read ↗

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

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

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

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

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

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

Translocation of proteins through the Sec61 and SecYEG channels.Semantic proximity Read ↗

Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes.Semantic proximity Read ↗

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

Dynamic action of the Sec machinery during initiation, protein translocation and termination.Semantic proximity Read ↗

The SecY translocation complex: convergence of genetics and structure.Semantic proximity Read ↗

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

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