Signal sequence recognition in posttranslational protein transport across the yeast ER membrane

被引:275
作者
Plath, K
Mothes, W
Wilkinson, BM
Stirling, CJ
Rapoport, TA [1 ]
机构
[1] Harvard Univ, Sch Med, Howard Hughes Med Inst, Boston, MA 02115 USA
[2] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA
[3] Univ Manchester, Sch Biol Sci, Manchester M13 9PT, Lancs, England
关键词
D O I
10.1016/S0092-8674(00)81738-9
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
We have analyzed how the signal sequence of prepor-alpha-factor is recognized during the first step of posttranslational protein transport into the yeast endoplasmic reticulum. Cross-linking studies indicate that the signal sequence interacts in a Kar2p- and ATP-independent reaction with Sec61p, the multispanning membrane component of the protein-conducting channel, by intercalation into transmembrane domains 2 and 7. While bound to Sec61p, the signal sequence forms a helix that is contacted on one side by Sec62p and Sec71p. The binding site is located at the interface of the protein channel and the lipid bilayer. Signal sequence recognition in cotranslational translocation in mammals appears to occur similarly. These results suggest a general mechanism by which the signal sequence could open the channel for polypeptide transport.
引用
收藏
页码:795 / 807
页数:13
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