Alignment of Conduits for the Nascent Polypeptide Chain in the Ribosome-Sec61 Complex

Author:

Beckmann Roland123,Bubeck Doryen123,Grassucci Robert123,Penczek Pawel123,Verschoor Adriana123,Blobel Günter123,Frank Joachim123

Affiliation:

1. R. Beckmann and G. Blobel, Howard Hughes Medical Institute, Laboratory of Cell Biology, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.

2. D. Bubeck, R. Grassucci, A. Verschoor, Wadsworth Center, New York State Department of Health, Empire State Plaza, Albany, NY 12201–0509, USA.

3. P. Penczek and J. Frank, Wadsworth Center, New York State Department of Health, and Department of Biomedical Sciences, State University of New York at Albany, Empire State Plaza, Albany, NY 12201–0509, USA.

Abstract

An oligomer of the Sec61 trimeric complex is thought to form the protein-conducting channel for protein transport across the endoplasmic reticulum. A purified yeast Sec61 complex bound to monomeric yeast ribosomes as an oligomer in a saturable fashion. Cryo–electron microscopy of the ribosome-Sec61 complex and a three-dimensional reconstruction showed that the Sec61 oligomer is attached to the large ribosomal subunit by a single connection. Moreover, a funnel-shaped pore in the Sec61 oligomer aligned with the exit of a tunnel traversing the large ribosomal subunit, strongly suggesting that both structures function together in the translocation of proteins across the endoplasmic reticulum membrane.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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