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

doi:10.1091/mbc.e03-06-0390

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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...

Topics

Biological Transport
Cell Compartmentation
Cloning, Molecular
Endoplasmic Reticulum
Intracellular Membranes
Mating Factor
Membrane Proteins
Membrane Transport Proteins
Mutation
Peptides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Binding

Protein Biosynthesis

Protein Precursors

Protein Processing, Post-Translational

Protein Sorting Signals

Protein Structure, Tertiary

SEC Translocation Channels

Saccharomyces cerevisiae

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Identifiers

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

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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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