Recent structural studies on Dom34/aPelota and Hbs1/aEF1α: important factors for solving general problems of ribosomal stall in translation.
Recent structural studies on Dom34/aPelota and Hbs1/aEF1α: important factors for solving general problems of ribosomal stall in translation.
复制标题
DOI：
10.2142/biophysics.9.131
复制
发表时间：
2013
期刊：
影响因子：
--
通讯作者：
Nureki O
中科院分区：
文献类型：
--
作者：
Kobayashi K;Ishitani R;Nureki O
在翻译过程中，翻译的核糖体通常在mRNA上移动，直到它们到达终止密码子。然而，当核糖体翻译异常的mRNA时，它们就会停滞不前。然后，核糖体被从异常的信使核糖核酸中解救出来，异常信使核糖体随后被降解。在真核生物中，Pelota(酵母菌中的Dom34)和Hbs1负责解决核糖体在翻译中停滞的一般问题。在古生菌中，分别与Pelota和Hbs1同源的aPelota和aEF1α被认为参与了这一过程。近年来，在确定Dom34/aPelota和Hbs1/aEF1α的结构方面取得了很大的进展。本文根据近年来核糖体结构的研究，重点介绍了Dom34/aPelota和HBS1/aEF1α在核糖体拯救中的功能作用。我们还将提出有待未来工作回答的问题。
In the translation process, translating ribosomes usually move on an mRNA until they reach the stop codon. However, when ribosomes translate an aberrant mRNA, they stall. Then, ribosomes are rescued from the aberrant mRNA, and the aberrant mRNA is subsequently degraded. In eukaryotes, Pelota (Dom34 in yeast) and Hbs1 are responsible for solving general problems of ribosomal stall in translation. In archaea, aPelota and aEF1α, homologous to Pelota and Hbs1, respectively, are considered to be involved in that process. In recent years, great progress has been made in determining structures of Dom34/aPelota and Hbs1/aEF1α. In this review, we focus on the functional roles of Dom34/aPelota and Hbs1/aEF1α in ribosome rescue, based on recent structural studies of them. We will also present questions to be answered by future work.