ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structural basis for mRNA surveillance by archaeal Pelota and GTP-bound EF1α complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed.
- The prospects of targeting messenger RNA surveillance factor PELOTA for developing virus resistance in plants.Plant molecular biology · 2026Review
- Ribosome-associated quality control of aberrant protein production during amino acid limitation.bioRxiv : the preprint server for biology · 2026Article
- Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025Review
- Gene Expression Signatures of Immaturity, Decreased pH, and Neural Hyperexcitation in the Hippocampus of Alzheimer's Disease Model Mice.Neuropsychopharmacology reports · 2025Article
- Novel archaeal ribosome dimerization factor facilitating unique 30S-30S dimerization.Nucleic acids research · 2025Article
- Article
- Co-Translational Quality Control Induced by Translational Arrest.Biomolecules · 2023Review
- Two modes of Cue2-mediated mRNA cleavage with distinct substrate recognition initiate no-go decay.Nucleic acids research · 2023Article
- RNA degradation is required for the germ-cell to maternal transition in Drosophila.Current biology : CB · 2021Article
- Detection and Degradation of Stalled Nascent Chains via Ribosome-Associated Quality Control.Annual review of biochemistry · 2020Review
- Switch of the interactions between the ribosomal stalk and EF1A in the GTP- and GDP-bound conformations.Scientific reports · 2019Article
- Extensions, Extra Factors, and Extreme Complexity: Ribosomal Structures Provide Insights into Eukaryotic Translation.Cold Spring Harbor perspectives in biology · 2019Review
- A specialised SKI complex assists the cytoplasmic RNA exosome in the absence of direct association with ribosomes.The EMBO journal · 2019Article
- In Silico Structural Modeling and Analysis of Elongation Factor-1 Alpha and Elongation Factor-like Protein.ACS omega · 2019Article
- The Origin and Evolution of Release Factors: Implications for Translation Termination, Ribosome Rescue, and Quality Control Pathways.International journal of molecular sciences · 2019Review
- Collided ribosomes form a unique structural interface to induce Hel2-driven quality control pathways.The EMBO journal · 2019Article
- Pelota-interacting G protein Hbs1 is required for spermatogenesis in Drosophila.Scientific reports · 2019Article
- Misdecoding of rare CGA codon by translation termination factors, eRF1/eRF3, suggests novel class of ribosome rescue pathway in S. cerevisiae.The FEBS journal · 2019Article
- A Pelota-like gene regulates root development and defence responses in rice.Annals of botany · 2018Article
- Ribosome recycling is coordinated by processive events in two asymmetric ATP sites of ABCE1.Life science alliance · 2018Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
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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