Recent structural studies on Dom34/aPelota and Hbs1/aEF1α: important factors for solving general problems of ribosomal stall in translation.

Biophysics (Nagoya-shi, Japan) Pub Date : 2013-09-07 eCollection Date: 2013-01-01 DOI:10.2142/biophysics.9.131
Kan Kobayashi, Ryuichiro Ishitani, Osamu Nureki
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引用次数: 5

Abstract

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.

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最近对Dom34/aPelota和Hbs1/aEF1α的结构研究:解决翻译中核糖体失速问题的重要因素。
在翻译过程中,翻译核糖体通常在mRNA上移动,直到到达停止密码子。然而,当核糖体翻译异常mRNA时,它们就会停止。然后,核糖体从异常mRNA中被解救出来,异常mRNA随后被降解。在真核生物中,Pelota(酵母中的Dom34)和Hbs1负责解决翻译中核糖体失位的一般问题。在古细菌中,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进展。本文基于近年来对Dom34/aPelota和Hbs1/aEF1α在核糖体拯救中的结构研究,对其功能作用进行综述。我们还将提出一些有待未来工作解答的问题。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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