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Article

Interactions between Sec complex and prepro-alpha-factor during posttranslational protein transport into the endoplasmic reticulum.

Molecular biology of the cell - 1 Jan 2004

Plath Kathrin, Wilkinson Barrie M, Stirling Colin J, Rapoport Tom A

Abstract excerpt

Posttranslational translocation of prepro-alpha-factor (ppalphaF) across the yeast endoplasmic reticulum membrane begins with the binding of the signal sequence to the Sec complex, a membrane component consisting of the trimeric Sec61p complex and the tetrameric Sec62p/63p complex. We show by photo-cross-linking that the signal sequence is bound directly to a site where it contacts simultaneously Sec61p and...

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

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Source

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Identifiers

PMID: 14617809
DOI: 10.1091/mbc.e03-06-0390
PMCID: PMC307522

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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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Interactions between Sec complex and prepro-alpha-factor during posttranslational protein transport into the endoplasmic reticulum.PMID 14617809Read ↗

Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p.Semantic proximity Read ↗

Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane.Semantic proximity Read ↗

The high affinity ATP binding site modulates the SecA-precursor interaction.Semantic proximity Read ↗

Structural studies and the assembly of the heptameric post-translational translocon complex.Semantic proximity Read ↗

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

BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum.Semantic proximity Read ↗

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

Sec62p, a component of the endoplasmic reticulum protein translocation machinery, contains multiple binding sites for the Sec-complex.Semantic proximity Read ↗

Specific transmembrane segments are selectively delayed at the ER translocon during opsin biogenesis.Semantic proximity Read ↗

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

Structure and folding of nascent polypeptide chains during protein translocation in the endoplasmic reticulum.Semantic proximity Read ↗

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

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