Structural basis for Spt5-mediated recruitment of the Paf1 complex to chromatin.

@article{Wier2013StructuralBF,
  title={Structural basis for Spt5-mediated recruitment of the Paf1 complex to chromatin.},
  author={Adam D. Wier and Manasi K. Mayekar and Annie H{\'e}roux and Karen M Arndt and Andrew P Vandemark},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2013},
  volume={110 43},
  pages={17290-5}
}
Polymerase associated factor 1 complex (Paf1C) broadly influences gene expression by regulating chromatin structure and the recruitment of RNA-processing factors during transcription elongation. The Plus3 domain of the Rtf1 subunit mediates Paf1C recruitment to genes by binding a repeating domain within the elongation factor Spt5 (suppressor of Ty). Here we provide a molecular description of this interaction by reporting the structure of human Rtf1 Plus3 in complex with a phosphorylated Spt5… CONTINUE READING
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