Kinetic mechanism of elongation factor Ts-catalyzed nucleotide exchange in elongation factor Tu.

@article{Gromadski2002KineticMO,
  title={Kinetic mechanism of elongation factor Ts-catalyzed nucleotide exchange in elongation factor Tu.},
  author={Kirill B Gromadski and Hans-Joachim Wieden and Marina V. Rodnina},
  journal={Biochemistry},
  year={2002},
  volume={41 1},
  pages={162-9}
}
The interaction of Escherichia coli elongation factor Tu (EF-Tu) with elongation factor Ts (EF-Ts) and guanine nucleotides was studied by the stopped-flow technique, monitoring the fluorescence of tryptophan 184 in EF-Tu or of the mant group attached to the guanine nucleotide. Rate constants of all association and dissociation reactions among EF-Tu, EF-Ts, GDP, and GTP were determined. EF-Ts enhances the dissociation of GDP and GTP from EF-Tu by factors of 6 x 10(4) and 3 x 10(3), respectively… CONTINUE READING

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