Structure of eEF3 and the mechanism of transfer RNA release from the E-site

@article{Andersen2006StructureOE,
  title={Structure of eEF3 and the mechanism of transfer RNA release from the E-site},
  author={Christian Brix Folsted Andersen and Thomas Becker and Michael Blau and Monika Anand and Mario Hali{\'c} and Bharvi Balar and Thorsten Mielke and Thomas Boesen and Jan Skov Pedersen and Christian M. T. Spahn and Terri Goss Kinzy and Gregers Rom Andersen and Roland Beckmann},
  journal={Nature},
  year={2006},
  volume={443},
  pages={663-668}
}
Elongation factor eEF3 is an ATPase that, in addition to the two canonical factors eEF1A and eEF2, serves an essential function in the translation cycle of fungi. eEF3 is required for the binding of the aminoacyl-tRNA–eEF1A–GTP ternary complex to the ribosomal A-site and has been suggested to facilitate the clearance of deacyl-tRNA from the E-site. Here we present the crystal structure of Saccharomyces cerevisiae eEF3, showing that it consists of an amino-terminal HEAT repeat domain, followed… 
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TLDR
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Mutations in the Chromodomain-like Insertion of Translation Elongation Factor 3 Compromise Protein Synthesis through Reduced ATPase Activity*
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TLDR
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TLDR
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Ribosome recycling step in yeast cytoplasmic protein synthesis is catalyzed by eEF3 and ATP
TLDR
It is shown that a Saccharomyces cerevisiae model PoTC was disassembled by ATP and eukaryotic elongation factor 3 (eEF3), and no 40S•mRNA complex was observed, indicating that eEF3 action promotes ribosome recycling, not reinitiation.
Directed hydroxyl radical probing reveals Upf1 binding to the 80S ribosomal E site rRNA at the L1 stalk
TLDR
The results shed light on the interaction between Upf1 and the ribosome, and suggest that upf1 may specifically engage a classical-state ribosomes during translation.
Ribosome profiling analysis of eEF3-depleted Saccharomyces cerevisiae
TLDR
Surprisingly, depletion of eEF3 leads to a relative decrease in P-site proline stalling, which is hypothesised to be a secondary effect of generally decreased translation and/or decreased competition for the E-site with eIF5A.
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