Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA

被引:101
作者
Prinz, A
Behrens, C
Rapoport, TA
Hartmann, E
Kalies, KU
机构
[1] Univ Gottingen, Zentrum Biochem & Mol Zellbiol, Biochem Abt 2, D-37073 Gottingen, Germany
[2] Harvard Univ, Sch Med, Howard Hughes Med Inst, Boston, MA 02115 USA
[3] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA
关键词
protein translocation; ribosome; rRNA; SecY; Sec61;
D O I
10.1093/emboj/19.8.1900
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
During early stages of cotranslational protein translocation across the endoplasmic reticulum (ER) membrane the ribosome is targeted to the heterotrimeric Sec61p complex, the major component of the protein-conducting channel. We demonstrate that this interaction is mediated by the 28S rRNA of the eukaryotic large ribosomal subunit. Bacterial ribosomes also bind via their 23S rRNA to the bacterial homolog of the Sec61p complex, the SecYEG complex. Eukaryotic ribosomes bind to the SecYEG complex, and prokaryotic ribosomes to the Sec61p complex. These data indicate that rRNA-mediated interaction of ribosomes with the translocation channel occurred early in evolution and has been conserved.
引用
收藏
页码:1900 / 1906
页数:7
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