pH-dependent conformational switch activates the inhibitor of transcription elongation.

@article{Laptenko2006pHdependentCS,
  title={pH-dependent conformational switch activates the inhibitor of transcription elongation.},
  author={Oleg Laptenko and Seung-Sup Kim and Jookyung J Lee and Marina Starodubtseva and Fellipe Cava and Jos{\'e} Berenguer and Xiang-Peng Kong and Sergei Borukhov},
  journal={The EMBO journal},
  year={2006},
  volume={25 10},
  pages={2131-41}
}
Gfh1, a transcription factor from Thermus thermophilus, inhibits all catalytic activities of RNA polymerase (RNAP). We characterized the Gfh1 structure, function and possible mechanism of action and regulation. Gfh1 inhibits RNAP by competing with NTPs for coordinating the active site Mg2+ ion. This coordination requires at least two aspartates at the tip of the Gfh1 N-terminal coiled-coil domain (NTD). The overall structure of Gfh1 is similar to that of the Escherichia coli transcript cleavage… CONTINUE READING

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