哺乳动物核糖体预终止复合物与 eRF1.eRF3.GDPNP 的结构。
Structure of the mammalian ribosomal pre-termination complex associated with eRF1.eRF3.GDPNP.
机构信息
Howard Hughes Medical Institute, Chevy Chase, MD, USA, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA, Department of Cell Biology, SUNY Downstate Medical Center, Brooklyn, NY, USA, Department of Pharmacology, Case Western Reserve University, Cleveland, OH, USA and Department of Biological Sciences, Columbia University, New York, NY, USA.
出版信息
Nucleic Acids Res. 2014 Mar;42(5):3409-18. doi: 10.1093/nar/gkt1279. Epub 2013 Dec 11.
Eukaryotic translation termination results from the complex functional interplay between two release factors, eRF1 and eRF3, in which GTP hydrolysis by eRF3 couples codon recognition with peptidyl-tRNA hydrolysis by eRF1. Here, we present a cryo-electron microscopy structure of pre-termination complexes associated with eRF1•eRF3•GDPNP at 9.7 -Å resolution, which corresponds to the initial pre-GTP hydrolysis stage of factor attachment and stop codon recognition. It reveals the ribosomal positions of eRFs and provides insights into the mechanisms of stop codon recognition and triggering of eRF3's GTPase activity.
真核翻译终止是由两个释放因子（eRF1 和 eRF3）之间复杂的功能相互作用产生的，其中 eRF3 的 GTP 水解将密码子识别与 eRF1 的肽酰-tRNA 水解偶联在一起。在这里，我们呈现了一个与 eRF1·eRF3·GDPNP 相关的终止前复合物的低温电子显微镜结构，分辨率为 9.7 -Å，对应于因子结合和终止密码子识别的初始预 GTP 水解阶段。它揭示了 eRFs 在核糖体上的位置，并深入了解了终止密码子识别和触发 eRF3 GTP 酶活性的机制。
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