English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  The Structure of Ribosome-Channel Complexes Engaged in Protein Translocation

Ménétret, J.-F., Neuhof, A., Morgan, D. G., Plath, K., Radermacher, M., Rapoport, T. A., et al. (2000). The Structure of Ribosome-Channel Complexes Engaged in Protein Translocation. Molecular Cell, 6(5), 1219-1232. doi:10.1016/S1097-2765(00)00118-0.

Item is

Files

show Files

Locators

show
hide
Locator:
Link (Any fulltext)
Description:
-
OA-Status:
Not specified

Creators

show
hide
 Creators:
Ménétret, Jean-François1, Author
Neuhof, Andrea1, Author
Morgan, David Gene1, Author
Plath, Kathrin1, Author
Radermacher, Michael2, Author           
Rapoport, Tom A1, Author
Akey, Christopher W.1, Author
Affiliations:
1External Organizations, ou_persistent22              
2Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              

Content

show
hide
Free keywords: -
 Abstract: Cotranslational translocation of proteins requires ribosome binding to the Sec61p channel at the endoplasmic reticulum (ER) membrane. We have used electron cryomicroscopy to determine the structures of ribosome-channel complexes in the absence or presence of translocating polypeptide chains. Surprisingly, the structures are similar and contain 3–4 connections between the ribosome and channel that leave a lateral opening into the cytosol. Therefore, the ribosome-channel junction may allow the direct transfer of polypeptides into the channel and provide a path for the egress of some nascent chains into the cytosol. Moreover, complexes solubilized from mammalian ER membranes contain an additional membrane protein that has a large, lumenal protrusion and is intercalated into the wall of the Sec61p channel. Thus, the native channel contains a component that is not essential for translocation.

Details

show
hide
Language(s): eng - English
 Dates: 2000-11
 Publication Status: Issued
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S1097-2765(00)00118-0
BibTex Citekey: menetret_structure_2000
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Molecular Cell
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 6 (5) Sequence Number: - Start / End Page: 1219 - 1232 Identifier: ISSN: 1097-2765
CoNE: https://pure.mpg.de/cone/journals/resource/954925610929