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…
157 Citations
eEF3 promotes late stages of tRNA translocation on the ribosome
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Cryo-EM analysis of ex vivo e EF3-ribosome complexes shows that eEF3 facilitates late steps of translocation by favoring non-rotated ribosomal states as well as by opening the L1 stalk to release the E-site tRNA.
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Background: Eukaryotic translation elongation factor 3 (eEF3) is a ribosome binding ATPase essential for fungal protein synthesis. Results: Mutations in the chromodomain-like insertion in an ATPase…
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Critical residues of the two ABC domains involved in nucleotide binding and hydrolysis were highly conserved in all the putative eEF3 homologs identified, supporting the functional role of the homologys as ATPases.
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- Biology, ChemistryProceedings of the National Academy of Sciences
- 2010
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.
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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.
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