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 Letters

Scoble, Judith¹  Ehrenberg, Måns¹  Dinçbaş, Vildan¹  Bilgin, Neş'e¹ 

[1] Department of Molecular Biology, BMC, Box 590, S-751 24, Uppsala, Sweden

关键词: GTP hydrolysis;    Translation;    Poly(Phe) synthesis;    Elongation factor Tu;    Ternary complex;    EF-Tu;    elongation factor Tu;    EF-G;    elongation factor G;    EF-Ts;    elongation factor Ts;    aa-tRNA;    aminoacyl transfer RNA;    Nac-Phe-tRNAPhe;    N-acetyl-phenyl-tRNAPhe;    TCA;    trichloroacetic acid;    RNase A;    ribonuclease A;   

DOI  :  10.1016/0014-5793(94)01318-U

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Recent observations indicate that the stoichiometry for the complex between EF-Tu · GTP and aminoacyl-tRNA (aa-tRNA) changes with temperature. At 37°C two EF-Tu · GTPs bind one aa-tRNA in an extended ternary complex, but at 0°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°C as well as at 0°C. This indicates two different pathways for the enzymatic binding of aa-tRNA to the A-site on the ribosome.

【 授权许可】

Unknown