A model for co-translational translocation: Ribosome-regulated nascent polypeptide translocation at the protein-conducting channel

被引：16
|
作者：
Mitra, Kakoh
Frank, Joachim
机构：
[1] New York State Dept Hlth, Wadsworth Ctr Labs & Res, Howard Hughes Med Inst, Hlth Res Inc, Albany, NY 12201 USA
[2] SUNY Albany, Dept Biomed Sci, Albany, NY 12201 USA
来源：
FEBS LETTERS | 2006年 / 580卷 / 14期
关键词：
signal sequence; transmembrane helix; membrane protein integration; translocase; post-translational translocation; SecA;
D O I：
10.1016/j.febslet.2006.05.019
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The protein-conducting channel (PCC) must allow both the translocation of soluble polypeptide regions across, and the lateral partitioning of hydrophobic transmembrane helices (TMHs) into, the membrane. We have analyzed existing structures of ribosomes and ribosome-PCC complexes and observe conformational changes suggesting that the ribosome may sense and orient the nascent polypeptide and also facilitate conformational changes in the PCC, subsequently directing the nascent polypeptide into the appropriate PCC-mediated translocation mode. The PCC is predicted to be able to accommodate one central, consolidated channel or two segregated pores with different lipid accessibilities, which may enable the lipid-mediated partitioning of a TMH from one pore, while the other, aqueous, pore allows trauslocation of a hydrophilic polypeptide segment. Our hypothesis suggests a plausible mechanism for the transitioning of the PCC between different configurations. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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页码：3353 / 3360
页数：8
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