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.
机构:
UNIV CALIF SAN FRANCISCO, MED CTR, DEPT BIOCHEM & BIOPHYS, SAN FRANCISCO, CA 94143 USAUNIV CALIF SAN FRANCISCO, MED CTR, DEPT BIOCHEM & BIOPHYS, SAN FRANCISCO, CA 94143 USA
DESHAIES, RJ
KIRSCHNER, M
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机构:
UNIV CALIF SAN FRANCISCO, MED CTR, DEPT BIOCHEM & BIOPHYS, SAN FRANCISCO, CA 94143 USAUNIV CALIF SAN FRANCISCO, MED CTR, DEPT BIOCHEM & BIOPHYS, SAN FRANCISCO, CA 94143 USA
机构:
UNIV CALIF SAN FRANCISCO, MED CTR, DEPT BIOCHEM & BIOPHYS, SAN FRANCISCO, CA 94143 USAUNIV CALIF SAN FRANCISCO, MED CTR, DEPT BIOCHEM & BIOPHYS, SAN FRANCISCO, CA 94143 USA
DESHAIES, RJ
KIRSCHNER, M
论文数: 0引用数: 0
h-index: 0
机构:
UNIV CALIF SAN FRANCISCO, MED CTR, DEPT BIOCHEM & BIOPHYS, SAN FRANCISCO, CA 94143 USAUNIV CALIF SAN FRANCISCO, MED CTR, DEPT BIOCHEM & BIOPHYS, SAN FRANCISCO, CA 94143 USA