Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1

@inproceedings{Musselman2012MolecularBF,
  title={Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1},
  author={Catherine A Musselman and Nikita Avvakumov and Reiko Watanabe and Christopher G. Abraham and Marie-Eve Lalonde and Zehui Hong and Christopher P. Allen and Siddhartha S. Roy and James K. Nu{\~n}ez and Jac A. Nickoloff and Caroline A. Kulesza and Akira Yasui and Jacques C{\^o}t{\'e} and Tatiana G Kutateladze},
  booktitle={Nature Structural &Molecular Biology},
  year={2012}
}
The PHD finger protein 1 (PHF1) is essential in epigenetic regulation and genome maintenance. Here we show that the Tudor domain of human PHF1 binds to histone H3 trimethylated at Lys36 (H3K36me3). We report a 1.9-Å resolution crystal structure of the Tudor domain in complex with H3K36me3 and describe the molecular mechanism of H3K36me3 recognition using NMR. Binding of PHF1 to H3K36me3 inhibits the ability of the Polycomb PRC2 complex to methylate Lys27 of histone H3 in vitro and in vivo… CONTINUE READING
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Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins

  • K Tripsianes
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