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Architecture of the ribosome-channel complex derived from native membranes.

Abstract：

:The mammalian Sec61 complex forms a protein translocation channel whose function depends upon its interaction with the ribosome and with membrane proteins of the endoplasmic reticulum (ER). To study these interactions, we determined structures of "native" ribosome-channel complexes derived from ER membranes. We find that the ribosome is linked to the channel by seven connections, but the junction may still provide a path for domains of nascent membrane proteins to move into the cytoplasm. In addition, the native channel is significantly larger than a channel formed by the Sec61 complex, due to the presence of a second membrane protein. We identified this component as TRAP, the translocon-associated protein complex. TRAP interacts with Sec61 through its transmembrane domain and has a prominent lumenal domain. The presence of TRAP in the native channel indicates that it may play a general role in translocation. Crystal structures of two Sec61 homologues were used to model the channel. This analysis indicates that there are four Sec61 complexes and two TRAP molecules in each native channel. Thus, we suggest that a single Sec61 complex may form a conduit for translocating polypeptides, while three copies of Sec61 play a structural role or recruit accessory factors such as TRAP.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Ménétret JF,Hegde RS,Heinrich SU,Chandramouli P,Ludtke SJ,Rapoport TA,Akey CW

doi

10.1016/j.jmb.2005.02.053

keywords:

subject

Has Abstract

pub_date

2005-04-29 00:00:00

pages

445-57

issue

2

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(05)00229-9

journal_volume

348

pub_type

杂志文章

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