Structural Basis for MRNA Surveillance by Archaeal Pelota and GTP-bound EF1α Complex

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2010 Sep 30

PMID 20876129

Citations 60

Authors

Kan Kobayashi

Izumi Kikuno

Kazushige Kuroha

Kazuki Saito

Koichi Ito

Ryuichiro Ishitani

Toshifumi Inada

Osamu Nureki

Affiliations

Soon will be listed here.

Abstract

No-go decay and nonstop decay are mRNA surveillance pathways that detect translational stalling and degrade the underlying mRNA, allowing the correct translation of the genetic code. In eukaryotes, the protein complex of Pelota (yeast Dom34) and Hbs1 translational GTPase recognizes the stalled ribosome containing the defective mRNA. Recently, we found that archaeal Pelota (aPelota) associates with archaeal elongation factor 1α (aEF1α) to act in the mRNA surveillance pathway, which accounts for the lack of an Hbs1 ortholog in archaea. Here we present the complex structure of aPelota and GTP-bound aEF1α determined at 2.3-Å resolution. The structure reveals how GTP-bound aEF1α recognizes aPelota and how aPelota in turn stabilizes the GTP form of aEF1α. Combined with the functional analysis in yeast, the present results provide structural insights into the molecular interaction between eukaryotic Pelota and Hbs1. Strikingly, the aPelota·aEF1α complex structurally resembles the tRNA·EF-Tu complex bound to the ribosome. Our findings suggest that the molecular mimicry of tRNA in the distorted "A/T state" conformation by Pelota enables the complex to efficiently detect and enter the empty A site of the stalled ribosome.

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