Curry Stephen, Kotik-Kogan Olga, Conte Maria R, Brick Peter
Biophysics Section, Blackett Laboratory, Imperial College, Exhibition Road, London, SW7 2AZ, UK.
Biochim Biophys Acta. 2009 Sep-Oct;1789(9-10):653-66. doi: 10.1016/j.bbagrm.2009.07.003. Epub 2009 Jul 18.
The specific recognition by proteins of the 5' and 3' ends of RNA molecules is an important facet of many cellular processes, including RNA maturation, regulation of translation initiation and control of gene expression by degradation and RNA interference. The aim of this review is to survey recent structural analyses of protein binding domains that specifically bind to the extreme 5' or 3' termini of RNA. For reasons of space and because their interactions are also governed by catalytic considerations, we have excluded enzymes that modify the 5' and 3' extremities of RNA. It is clear that there is enormous structural diversity among the proteins that have evolved to bind to the ends of RNA molecules. Moreover, they commonly exhibit conformational flexibility that appears to be important for binding and regulation of the interaction. This flexibility has sometimes complicated the interpretation of structural results and presents significant challenges for future investigations.
蛋白质对RNA分子5'端和3'端的特异性识别是许多细胞过程的一个重要方面，包括RNA成熟、翻译起始调控以及通过降解和RNA干扰对基因表达的控制。本综述的目的是概述蛋白质结合结构域的近期结构分析，这些结构域特异性结合RNA的极端5'或3'末端。出于篇幅考虑，并且由于它们的相互作用也受催化因素的支配，我们排除了修饰RNA 5'和3'末端的酶。显然，在进化过程中能够结合RNA分子末端的蛋白质之间存在巨大的结构多样性。此外，它们通常表现出构象灵活性，这似乎对结合和相互作用的调节很重要。这种灵活性有时使结构结果的解释变得复杂，并给未来的研究带来了重大挑战。
