Cotranslational protein integration into the ER membrane is mediated by the binding of nascent chains to translocon proteins

McCormick, Peter J., Miao, Yiwei, Shao, Yuanlong, Lin, Jialing and Johnson, Arthur E. (2003) Cotranslational protein integration into the ER membrane is mediated by the binding of nascent chains to translocon proteins. Molecular Cell, 12 (2). pp. 329-341. ISSN 1097-2765

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Abstract

During cotranslational protein integration into the ER membrane, each transmembrane (TM) segment moves laterally through the translocon to reach the lipid bilayer. Photocrosslinking studies reveal that a particular surface of each nascent chain TM α helix and signal-anchor sequence always faces Sec61α in the translocon. This nonrandom and TM sequence-dependent positioning reveals that each TM segment makes specific contacts with Sec61α and is retained at a fixed location within the translocon, observations that are best explained by the binding of each TM sequence to a translocon protein(s). Since TM sequence hydrophobicity does not correlate with its rate of release from the translocon, nascent chain movement through the translocon appears to be mediated primarily by protein-protein interactions rather than hydrophobic nascent chain-phospholipid interactions.

Item Type: Article
Faculty \ School: Faculty of Science > School of Pharmacy
Related URLs:
Depositing User: Pure Connector
Date Deposited: 13 Jan 2014 13:42
Last Modified: 21 Apr 2020 22:45
URI: https://ueaeprints.uea.ac.uk/id/eprint/47166
DOI: 10.1016/S1097-2765(03)00304-6

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