Crystal structures of the S. cerevisiae Spt6 core and C-terminal tandem SH2 domain.

@article{Close2011CrystalSO,
  title={Crystal structures of the S. cerevisiae Spt6 core and C-terminal tandem SH2 domain.},
  author={Devin W. Close and Sean J Johnson and Matthew A Sdano and Seth M McDonald and Howard Robinson and Tim Formosa and Christopher P Hill},
  journal={Journal of molecular biology},
  year={2011},
  volume={408 4},
  pages={697-713}
}
The conserved and essential eukaryotic protein Spt6 functions in transcription elongation, chromatin maintenance, and RNA processing. Spt6 has three characterized functions. It is a histone chaperone capable of reassembling nucleosomes, a central component of transcription elongation complexes, and is required for recruitment of RNA processing factors to elongating RNA polymerase II (RNAPII). Here, we report multiple crystal structures of the 168-kDa Spt6 protein from Saccharomyces cerevisiae… CONTINUE READING

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