Nucleosome contact triggers conformational changes of Rpd3S driving high-affinity H3K36me nucleosome engagement.

  title={Nucleosome contact triggers conformational changes of Rpd3S driving high-affinity H3K36me nucleosome engagement.},
  author={C. Ruan and C. Lee and Haochen Cui and S. Li and B. Li},
  journal={Cell reports},
  volume={10 2},
  • C. Ruan, C. Lee, +2 authors B. Li
  • Published 2015
  • Biology, Medicine
  • Cell reports
  • The Rpd3S histone deacetylase complex utilizes two subunits, Eaf3 and Rco1, to recognize nucleosomes methylated at H3K36 (H3K36me) with high affinity and strong specificity. However, the chromobarrel domain of Eaf3 (CHD) that is responsible for H3K36me recognition only binds weakly and with little specificity to histone peptides. Here, using deuterium exchange mass spectrometry (DXMS), we detected conformational changes of Rpd3S upon its contact with chromatin. Interestingly, we found that the… CONTINUE READING
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