Structural basis for mRNA surveillance by archaeal Pelota and GTP-bound EF1α complex

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 1 alpha (aEF1 alpha) 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 aEF1 alpha determined at 2.3-A resolution. The structure reveals how GTP-bound aEF1 alpha recognizes aPelota and how aPelota in turn stabilizes the GTP form of aEF1 alpha. 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 center dot aEF1 alpha complex structurally resembles the tRNA center dot 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.