Peluso P, Herschlag D, Nock S, Freymann D M, Johnson A E, Walter P
Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143, USA.
Science. 2000 Jun 2;288(5471):1640-3. doi: 10.1126/science.288.5471.1640.
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.
信号识别颗粒(SRP)及其受体介导蛋白质靶向内质网或细菌质膜的机制在进化上是保守的。在大肠杆菌中,该反应由Ffh/4.5S RNA核糖核蛋白复合物(Ffh/4.5S RNP;即SRP)和FtsY蛋白(SRP受体)介导。我们通过监测色氨酸荧光的变化来量化4.5S RNA对Ffh-FtsY复合物形成的影响。令人惊讶的是,4.5S RNA在相似程度上促进了Ffh-FtsY复合物的组装和解聚。这些结果提供了一个RNA分子以催化方式促进蛋白质-蛋白质相互作用的例子。