PMID:8001671
| Citation |
Dinçbaş, V, Bilgin, N, Scoble, J and Ehrenberg, M (1995) Two GTPs are consumed on EF-Tu per peptide bond in poly(Phe) synthesis, in spite of switching stoichiometry of the EF-Tu.aminoacyl-tRNA complex with temperature. FEBS Lett. 357:19-22 |
|---|---|
| Abstract |
Recent observations indicate that the stoichiometry for the complex between EF-Tu.GTP and aminoacyl-tRNA (aa-tRNA) changes with temperature. At 37 degrees C two EF-Tu.GTPs bind one aa-tRNA in an extended ternary complex, but at 0 degrees C the complex has 1:1 stoichiometry. However, the present experiments show that there are two GTPs hydrolyzed on EF-Tu per peptide bond in poly(Phe) synthesis at 37 degrees C as well as at 0 degrees C. This indicates two different pathways for the enzymatic binding of aa-tRNA to the A-site on the ribosome. |
| Links | |
| Keywords |
Escherichia coli; Guanosine Triphosphate/metabolism; Molecular Conformation; Peptide Biosynthesis; Peptide Chain Elongation, Translational; Peptide Elongation Factor Tu/chemistry; Peptide Elongation Factor Tu/metabolism; Peptides; Phenylalanine/metabolism; Protein Binding; RNA, Transfer, Amino Acyl/chemistry; RNA, Transfer, Amino Acyl/metabolism; Temperature |
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