Abstract
No-go decay (NGD) and Nonstop decay (NSD) are mRNA surveillance pathways that detect the stalled ribosome containing the defective mRNA. In archaea, archaeal Pelota (aPelota) associates with archaeal elongation factor 1α (aEF1α) to act in the mRNA surveillance pathway. Here, we present the complex structure of aPelota and GTP-bound aEF1α determined at 2.3 Å resolution. Notably, the aPelota·aEF1α·GTP complex structurally resembles the tRNA·EF-Tu complex bound to the ribosome. Combined with the functional analysis in yeast, our findings provide structural insights into how aPelota·aEF1α·GTP complex detects the stalled ribosome and triggers NGD and NSD.
