Catalytic effects of elongation factor Ts on polypeptide synthesis

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Abstract
The kinetic parameters which characterize the interaction between elongation factor Tu (EF‐Tu) and elongation factor Ts (EF‐Ts) have been determined in a poly(uridylic acid)‐primed translation system. The EF‐Ts catalyzed release of GDP from EF‐Tu was measured independently in a nucleotide exchange assay. We conclude that the rate‐limiting step for the EF‐Tu cycle in protein synthesis in the absence of EF‐Ts is the release of GDP. By adding EF‐Ts the time of this step is reduced from 90 s to 30 ms. Half maximal rate is obtained at an EF‐Ts concentration of 2.5 x 10−6 M.