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
- 2 January 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 357 (1), 19-22
- https://doi.org/10.1016/0014-5793(94)01318-u
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.Keywords
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