Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation

Dorit Hanein; Kent E.S. Matlack; Berit Jungnickel; Kathrin Plath; Kai Uwe Kalies; Kenneth R. Miller; Tom A. Rapoport; Christopher W. Akey

doi:10.1016/S0092-8674(00)81391-4

Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation

Dorit Hanein^*, Kent E.S. Matlack, Berit Jungnickel, Kathrin Plath, Kai Uwe Kalies, Kenneth R. Miller, Tom A. Rapoport, Christopher W. Akey

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Biologie

283 Zitate (Scopus)

Abstract

The heterotrimeric Sec61p complex is a major component of the protein- conducting channel of the endoplasmic reticulum (ER) membrane, associating with either ribosomes or the Sec62/63 complex to perform co- and posttranslational transport, respectively. We show by electron microscopy that purified mammalian and yeast Sec61p complexes in detergent form cylindrical oligomers with a diameter of ~85Å and a central pore of ~20 Å. Each oligomer contains 3-4 heterotrimers. Similar ring structures are seen in reconstituted proteoliposomes and native membranes. Oligomer formation by the reconstituted Sec61p complex is stimulated by its association with ribosomes or the Sec62/63p complex. We propose that these cylindrical oligomers represent protein-conducting channels of the ER, formed by ligands specific for co- and post-translational transport.

Originalsprache	Englisch
Zeitschrift	Cell
Jahrgang	87
Ausgabenummer	4
Seiten (von - bis)	721-732
Seitenumfang	12
ISSN	0092-8674
DOIs	https://doi.org/10.1016/S0092-8674(00)81391-4
Publikationsstatus	Veröffentlicht - 15.01.1996

Fördermittel

This work was supported by NIH grants to C. W. A. and T. A. R., the Fulbright Junior Research Program (D. H.), and a Rothschild Fellowship (D. H.). We thank Dr. J. Wall and M. Simon for collecting scanning-transmission electron microscopy images analyzed in this work, and Dr. E. Bullitt for help with the Brandeis mass-analysis programs. We thank M. Rolls, P. Stein, and E. Hartmann for critical reading of the manuscript.

UN SDGs

Dieser Output leistet einen Beitrag zu folgendem(n) Ziel(en) für nachhaltige Entwicklung

SDG 3 – Gesundheit und Wohlergehen

Strategische Forschungsbereiche und Zentren

Forschungsschwerpunkt: Infektion und Entzündung - Zentrum für Infektions- und Entzündungsforschung Lübeck (ZIEL)

Dokumente

10.1016/S0092-8674(00)81391-4

Weitere Links

Link to publication in Scopus

Zitieren

@article{be3c9b25667d4880b078469db6d911e4,

title = "Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation",

abstract = "The heterotrimeric Sec61p complex is a major component of the protein- conducting channel of the endoplasmic reticulum (ER) membrane, associating with either ribosomes or the Sec62/63 complex to perform co- and posttranslational transport, respectively. We show by electron microscopy that purified mammalian and yeast Sec61p complexes in detergent form cylindrical oligomers with a diameter of \textasciitilde{}85{\AA} and a central pore of \textasciitilde{}20 {\AA}. Each oligomer contains 3-4 heterotrimers. Similar ring structures are seen in reconstituted proteoliposomes and native membranes. Oligomer formation by the reconstituted Sec61p complex is stimulated by its association with ribosomes or the Sec62/63p complex. We propose that these cylindrical oligomers represent protein-conducting channels of the ER, formed by ligands specific for co- and post-translational transport.",

author = "Dorit Hanein and Matlack, \{Kent E.S.\} and Berit Jungnickel and Kathrin Plath and Kalies, \{Kai Uwe\} and Miller, \{Kenneth R.\} and Rapoport, \{Tom A.\} and Akey, \{Christopher W.\}",

note = "Funding Information: This work was supported by NIH grants to C. W. A. and T. A. R., the Fulbright Junior Research Program (D. H.), and a Rothschild Fellowship (D. H.). We thank Dr. J. Wall and M. Simon for collecting scanning-transmission electron microscopy images analyzed in this work, and Dr. E. Bullitt for help with the Brandeis mass-analysis programs. We thank M. Rolls, P. Stein, and E. Hartmann for critical reading of the manuscript. Copyright: Copyright 2021 Elsevier B.V., All rights reserved.",

year = "1996",

month = jan,

day = "15",

doi = "10.1016/S0092-8674(00)81391-4",

language = "English",

volume = "87",

pages = "721--732",

journal = "Cell",

issn = "0092-8674",

publisher = "Cell Press",

number = "4",

}

TY - JOUR

T1 - Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation

AU - Hanein, Dorit

AU - Matlack, Kent E.S.

AU - Jungnickel, Berit

AU - Plath, Kathrin

AU - Kalies, Kai Uwe

AU - Miller, Kenneth R.

AU - Rapoport, Tom A.

AU - Akey, Christopher W.

N1 - Funding Information: This work was supported by NIH grants to C. W. A. and T. A. R., the Fulbright Junior Research Program (D. H.), and a Rothschild Fellowship (D. H.). We thank Dr. J. Wall and M. Simon for collecting scanning-transmission electron microscopy images analyzed in this work, and Dr. E. Bullitt for help with the Brandeis mass-analysis programs. We thank M. Rolls, P. Stein, and E. Hartmann for critical reading of the manuscript. Copyright: Copyright 2021 Elsevier B.V., All rights reserved.

PY - 1996/1/15

Y1 - 1996/1/15

N2 - The heterotrimeric Sec61p complex is a major component of the protein- conducting channel of the endoplasmic reticulum (ER) membrane, associating with either ribosomes or the Sec62/63 complex to perform co- and posttranslational transport, respectively. We show by electron microscopy that purified mammalian and yeast Sec61p complexes in detergent form cylindrical oligomers with a diameter of ~85Å and a central pore of ~20 Å. Each oligomer contains 3-4 heterotrimers. Similar ring structures are seen in reconstituted proteoliposomes and native membranes. Oligomer formation by the reconstituted Sec61p complex is stimulated by its association with ribosomes or the Sec62/63p complex. We propose that these cylindrical oligomers represent protein-conducting channels of the ER, formed by ligands specific for co- and post-translational transport.

AB - The heterotrimeric Sec61p complex is a major component of the protein- conducting channel of the endoplasmic reticulum (ER) membrane, associating with either ribosomes or the Sec62/63 complex to perform co- and posttranslational transport, respectively. We show by electron microscopy that purified mammalian and yeast Sec61p complexes in detergent form cylindrical oligomers with a diameter of ~85Å and a central pore of ~20 Å. Each oligomer contains 3-4 heterotrimers. Similar ring structures are seen in reconstituted proteoliposomes and native membranes. Oligomer formation by the reconstituted Sec61p complex is stimulated by its association with ribosomes or the Sec62/63p complex. We propose that these cylindrical oligomers represent protein-conducting channels of the ER, formed by ligands specific for co- and post-translational transport.

UR - https://www.scopus.com/pages/publications/0345444027

U2 - 10.1016/S0092-8674(00)81391-4

DO - 10.1016/S0092-8674(00)81391-4

M3 - Journal articles

C2 - 8929540

AN - SCOPUS:0345444027

SN - 0092-8674

VL - 87

SP - 721

EP - 732

JO - Cell

JF - Cell

IS - 4

ER -

Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation

Abstract

Fördermittel

UN SDGs

Strategische Forschungsbereiche und Zentren

Dokumente

Weitere Links

Fingerprint

Zitieren