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

被引:269
作者
Hanein, D
Matlack, KES
Jungnickel, B
Plath, K
Kalies, KU
Miller, KR
Rapoport, TA
Akey, CW
机构
[1] HARVARD UNIV,SCH MED,DEPT CELL BIOL,BOSTON,MA 02115
[2] MAX DELBRUCK CTR MOL MED,D-13122 BERLIN,GERMANY
[3] BROWN UNIV,DIV BIOL & MED,PROVIDENCE,RI 02912
基金
美国国家卫生研究院;
关键词
D O I
10.1016/S0092-8674(00)81391-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 similar to 85 Angstrom and a central pore of similar to 20 Angstrom. 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 posttranslational transport.
引用
收藏
页码:721 / 732
页数:12
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