Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptor

被引：124

作者：

Peluso, P

Herschlag, D

Nock, S

Freymann, DM

Johnson, AE

Walter, P ^{[1
]}

机构：

[1] Univ Calif San Francisco, Howard Hughes Med Inst, San Francisco, CA 94143 USA

[2] Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USA

[3] Stanford Univ, Dept Biochem, Stanford, CA 94305 USA

[4] Texas A&M Univ, Syst Hlth Sci Ctr, College Stn, TX 77843 USA

来源：

SCIENCE | 2000年 / 288卷 / 5471期

关键词：

D O I：

10.1126/science.288.5471.1640

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：

The mechanism by which a signal recognition particle (SRP) and its receptor mediate protein targeting to the endoplasmic reticulum or to the bacterial plasma membrane is evolutionarily conserved. in Escherichia coli, this reaction is mediated by the Ffh/4.5S RNA ribonucleoprotein complex (Ffh/4.5S RNP; the SRP) and the FtsY protein (the SRP receptor). We have quantified the effects of 4.5S RNA on Ffh-FtsY complex formation by monitoring changes in tryptophan fluorescence. Surprisingly, 4.5S RNA facilitates both assembly and disassembly of the Ffh-FtsY complex to a similar extent. These results provide an example of an RNA molecule facilitating protein-protein interactions in a catalytic fashion.

引用

页码：1640 / 1643

页数：4

共 27 条

[1] Crystal structure of the ribonucleoprotein core of the signal recognition particle [J].