Structural, biochemical, and dynamic characterizations of the hRPB8 subunit of human RNA polymerases.

@article{Kang2006StructuralBA,
  title={Structural, biochemical, and dynamic characterizations of the hRPB8 subunit of human RNA polymerases.},
  author={Xue Kang and Yunfei Hu and You Xiang Li and Xianrong Guo and Xiaolu Jiang and Luhua Lai and Bin Xia and Changwen Jin},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 26},
  pages={18216-26}
}
The RPB8 subunit is present in all three types of eukaryotic RNA polymerases and is highly conserved during evolution. It is an essential subunit required for the transcription of nuclear genes, but the detailed mechanism including its interactions with different subunits and oligonucleotides remains largely unclear. Herein, we report the three-dimensional structure of human RPB8 (hRPB8) at high resolution determined by NMR spectroscopy. The protein fold comprises an eight-stranded beta-barrel… CONTINUE READING

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Solution Structure of hRPB8 18226 JOURNAL OF BIOLOGICAL CHEMISTRY VOLUME

P. Gouet, E. Courcelle, D. I. Stuart, F. andMetoz
JUNE 30, • 2006
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