Yeast Sec proteins interact with polypeptides traversing the endoplasmic reticulum membrane

Anne Müsch; Martin Wiedmann; Tom A. Rapoport

doi:10.1016/0092-8674(92)90414-8

Yeast Sec proteins interact with polypeptides traversing the endoplasmic reticulum membrane

Anne Müsch, Martin Wiedmann, Tom A. Rapoport

Research output: Contribution to journal › Article › peer-review

109 Scopus citations

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 language	English (US)
Pages (from-to)	343-352
Number of pages	10
Journal	Cell
Volume	69
Issue number	2
DOIs	https://doi.org/10.1016/0092-8674(92)90414-8
State	Published - Apr 17 1992
Externally published	Yes

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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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 M{\"u}sch and Martin Wiedmann and Rapoport, {Tom A.}",

note = "Funding Information: blatt, and R. Schekman for the generous supply of antibodies to the a factor and Set proteins. We also thank many colleagues for helpful comments on various versions of the manuscript. The work was supported by the DFG (grant Ra 518/l-2). Copyright: Copyright 2015 Elsevier B.V., All rights reserved.",

year = "1992",

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doi = "10.1016/0092-8674(92)90414-8",

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

AU - Müsch, Anne

AU - Wiedmann, Martin

AU - Rapoport, Tom A.

N1 - Funding Information: blatt, and R. Schekman for the generous supply of antibodies to the a factor and Set proteins. We also thank many colleagues for helpful comments on various versions of the manuscript. The work was supported by the DFG (grant Ra 518/l-2). Copyright: Copyright 2015 Elsevier B.V., All rights reserved.

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.

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Yeast Sec proteins interact with polypeptides traversing the endoplasmic reticulum membrane

Abstract

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