Yeast Sec proteins interact with polypeptides traversing the endoplasmic reticulum membrane

Anne Muesch, Martin Wiedmann, Tom A. Rapoport

Research output: Contribution to journalArticle

82 Citations (Scopus)

Abstract

We show by photocross-linking that nascent secretory proteins, during their passage through the endoplasmic reticulum membrane of S. cerevisiae, are in physical contact with Sec61p and Sec62p, two genetically identified membrane proteins that are essential for in vivo translocation. Sec61p seems to be in continuous contact, whereas Sec62p is involved only transiently. Translocation comprises both ATP-dependent and -independent phases of interaction with the Sec proteins. The results suggest a direct role of the Sec proteins in translocation.

Original languageEnglish (US)
Pages (from-to)343-352
Number of pages10
JournalCell
Volume69
Issue number2
DOIs
StatePublished - Apr 17 1992
Externally publishedYes

Fingerprint

Fungal Proteins
Endoplasmic Reticulum
Membranes
Peptides
Protein Transport
Saccharomyces cerevisiae
Membrane Proteins
Proteins
Adenosine Triphosphate

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

Yeast Sec proteins interact with polypeptides traversing the endoplasmic reticulum membrane. / Muesch, Anne; Wiedmann, Martin; Rapoport, Tom A.

In: Cell, Vol. 69, No. 2, 17.04.1992, p. 343-352.

Research output: Contribution to journalArticle

Muesch, Anne ; Wiedmann, Martin ; Rapoport, Tom A. / Yeast Sec proteins interact with polypeptides traversing the endoplasmic reticulum membrane. In: Cell. 1992 ; Vol. 69, No. 2. pp. 343-352.
@article{c095353602fb4829aaf634de8463a025,
title = "Yeast Sec proteins interact with polypeptides traversing the endoplasmic reticulum membrane",
abstract = "We show by photocross-linking that nascent secretory proteins, during their passage through the endoplasmic reticulum membrane of S. cerevisiae, are in physical contact with Sec61p and Sec62p, two genetically identified membrane proteins that are essential for in vivo translocation. Sec61p seems to be in continuous contact, whereas Sec62p is involved only transiently. Translocation comprises both ATP-dependent and -independent phases of interaction with the Sec proteins. The results suggest a direct role of the Sec proteins in translocation.",
author = "Anne Muesch and Martin Wiedmann and Rapoport, {Tom A.}",
year = "1992",
month = "4",
day = "17",
doi = "10.1016/0092-8674(92)90414-8",
language = "English (US)",
volume = "69",
pages = "343--352",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "2",

}

TY - JOUR

T1 - Yeast Sec proteins interact with polypeptides traversing the endoplasmic reticulum membrane

AU - Muesch, Anne

AU - Wiedmann, Martin

AU - Rapoport, Tom A.

PY - 1992/4/17

Y1 - 1992/4/17

N2 - We show by photocross-linking that nascent secretory proteins, during their passage through the endoplasmic reticulum membrane of S. cerevisiae, are in physical contact with Sec61p and Sec62p, two genetically identified membrane proteins that are essential for in vivo translocation. Sec61p seems to be in continuous contact, whereas Sec62p is involved only transiently. Translocation comprises both ATP-dependent and -independent phases of interaction with the Sec proteins. The results suggest a direct role of the Sec proteins in translocation.

AB - We show by photocross-linking that nascent secretory proteins, during their passage through the endoplasmic reticulum membrane of S. cerevisiae, are in physical contact with Sec61p and Sec62p, two genetically identified membrane proteins that are essential for in vivo translocation. Sec61p seems to be in continuous contact, whereas Sec62p is involved only transiently. Translocation comprises both ATP-dependent and -independent phases of interaction with the Sec proteins. The results suggest a direct role of the Sec proteins in translocation.

UR - http://www.scopus.com/inward/record.url?scp=0026528370&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026528370&partnerID=8YFLogxK

U2 - 10.1016/0092-8674(92)90414-8

DO - 10.1016/0092-8674(92)90414-8

M3 - Article

C2 - 1568249

AN - SCOPUS:0026528370

VL - 69

SP - 343

EP - 352

JO - Cell

JF - Cell

SN - 0092-8674

IS - 2

ER -