Abstract
In the elongation cycle of bacterial protein synthesis the interaction between elongation factor-Tu (EF-Tu)⋅guanosine triphosphate (GTP), aminoacyl-transfer RNA (aa-tRNA), and messenger RNA-programmed ribosomes is associated with the hydrolysis of GTP. This interaction determines the selection of the proper aa-tRNA for incorporation into the polypeptide. In the canonical scheme, one molecule of GTP is hydrolyzed in the EF-Tu-dependent binding of aa-tRNA to the ribosome, and a second molecule is hydrolyzed in the elongation factor-G (EF-G)-mediated translocation of the polypeptide from the ribosomal A site to the P site. Substitution of Asp 138 with Asn in EF-Tu changed the substrate specificity from GTP to xanthosine triphosphate and demonstrated that the EF-Tu-mediated reactions involved the hydrolysis of two nucleotide triphosphates for each Phe incorporated. This stoichiometry of two is associated with the binding of the correct aa-tRNA to the ribosome.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 7:05 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 15, 2024, 5:18 a.m.) |
Indexed | 1 month, 4 weeks ago (July 2, 2025, 2:46 p.m.) |
Issued | 32 years, 6 months ago (Feb. 26, 1993) |
Published | 32 years, 6 months ago (Feb. 26, 1993) |
Published Print | 32 years, 6 months ago (Feb. 26, 1993) |
@article{Weijland_1993, title={Toward a Model for the Interaction Between Elongation Factor Tu and the Ribosome}, volume={259}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.8446899}, DOI={10.1126/science.8446899}, number={5099}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Weijland, Albert and Parmeggiani, Andrea}, year={1993}, month=feb, pages={1311–1314} }