Signal recognition particle receptor exposes the ribosomal translocon binding site

被引：111
作者：
Halic, M
Gartmann, M
Schlenker, O
Mielke, T
Pool, MR
Sinning, I
Beckmann, R
机构：
[1] Univ Med Sch Berlin, Charite, Inst Biochem, D-10117 Berlin, Germany
[2] Univ Heidelberg, Biochem Ctr BZH, D-69120 Heidelberg, Germany
[3] Max Planck Inst Mol Genet, Ultrastruct Network, USN, D-14195 Berlin, Germany
[4] Univ Manchester, Fac Life Sci, Manchester M13 9PT, Lancs, England
来源：
SCIENCE | 2006年 / 312卷 / 5774期
关键词：
D O I：
10.1126/science.1124864
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Signal sequences of secretory and membrane proteins are recognized by the signal recognition particle (SRP) as they emerge from the ribosome. This results in their targeting to the membrane by docking with the SRP receptor, which facilitates transfer of the ribosome to the translocon. Here, we present the 8 angstrom cryo - electron microscopy structure of a "docking complex'' consisting of a SRP-bound 80S ribosome and the SRP receptor. Interaction of the SRP receptor with both SRP and the ribosome rearranged the S domain of SRP such that a ribosomal binding site for the translocon, the L23e/L35 site, became exposed, whereas Alu domain - mediated elongation arrest persisted.
引用
收藏
页码：745 / 747
页数：3
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