Thermodynamic characterization of ppGpp binding to EF-G or IF2 and of initiator tRNA binding to free IF2 in the presence of GDP, GTP, or ppGpp.

@article{Mitkevich2010ThermodynamicCO,
  title={Thermodynamic characterization of ppGpp binding to EF-G or IF2 and of initiator tRNA binding to free IF2 in the presence of GDP, GTP, or ppGpp.},
  author={Vladimir A Mitkevich and Andrey B. Ermakov and Alexandra A Kulikova and Stoyan Tankov and Viktoriya Shyp and Aksel Soosaar and Tanel Tenson and Alexander A. Makarov and M{\aa}ns Ehrenberg and Vasili Hauryliuk},
  journal={Journal of molecular biology},
  year={2010},
  volume={402 5},
  pages={
          838-46
        }
}
In addition to their natural substrates GDP and GTP, the bacterial translational GTPases initiation factor (IF) 2 and elongation factor G (EF-G) interact with the alarmone molecule guanosine tetraphosphate (ppGpp), which leads to GTPase inhibition. We have used isothermal titration calorimetry to determine the affinities of ppGpp for IF2 and EF-G at a temperature interval of 5-25 °C. We find that ppGpp has a higher affinity for IF2 than for EF-G (1.7-2.8 μM K(d)versus 9.1-13.9 μM K(d) at 10-25… CONTINUE READING

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Diversity in (p)ppGpp metabolism and effectors.

Current opinion in microbiology • 2015
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