Kieft Jeffrey S
Department of Biochemistry and Molecular Genetics, University of Colorado Denver School of Medicine, Mail stop 8101, PO Box 6511, Aurora, CO 80045, USA.
Trends Biochem Sci. 2008 Jun;33(6):274-83. doi: 10.1016/j.tibs.2008.04.007. Epub 2008 May 28.
In eukaryotes, protein synthesis initiates primarily by a mechanism that requires a modified nucleotide 'cap' on the mRNA and also proteins that recruit and position the ribosome. Many pathogenic viruses use an alternative, cap-independent mechanism that substitutes RNA structure for the cap and many proteins. The RNAs driving this process are called internal ribosome-entry sites (IRESs) and some are able to bind the ribosome directly using a specific 3D RNA structure. Recent structures of IRES RNAs and IRES-ribosome complexes are revealing the structural basis of viral IRES' 'hijacking' of the protein-making machinery. It now seems that there are fundamental differences in the 3D structures used by different IRESs, although there are some common features in how they interact with ribosomes.
在真核生物中,蛋白质合成主要通过一种机制启动,该机制需要mRNA上的一种修饰核苷酸“帽”以及招募和定位核糖体的蛋白质。许多致病病毒使用一种替代的、不依赖帽的机制,该机制用RNA结构替代帽和许多蛋白质。驱动这一过程的RNA被称为内部核糖体进入位点(IRES),其中一些能够利用特定的三维RNA结构直接结合核糖体。IRES RNA和IRES-核糖体复合物的最新结构揭示了病毒IRES“劫持”蛋白质制造机器的结构基础。现在看来,不同IRES使用的三维结构存在根本差异,尽管它们与核糖体相互作用的方式有一些共同特征。