Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast

@article{Sun2002UbiquitinationOH,
  title={Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast},
  author={Zu-Wen Sun and C. David Allis},
  journal={Nature},
  year={2002},
  volume={418},
  pages={104-108}
}
In eukaryotes, the DNA of the genome is packaged with histone proteins to form nucleosomal filaments, which are, in turn, folded into a series of less well understood chromatin structures. Post-translational modifications of histone tail domains modulate chromatin structure and gene expression. Of these, histone ubiquitination is poorly understood. Here we show that the ubiquitin-conjugating enzyme Rad6 (Ubc2) mediates methylation of histone H3 at lysine 4 (Lys 4) through ubiquitination of H2B… 
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An intrinsic difference in the property of chromatin assembled in the presence or absence of H2Bub1 is revealed and the regulation of nucleosome stability is implicates as the mechanism by which H2 Bub1 modulates nucleosomes dynamics and histone methylation during transcription.
Deubiquitination of Histone H2B by a Yeast Acetyltransferase Complex Regulates Transcription*
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It is found that, contrary to expectations, H2B is extensively polyubiquitylated, raising the possibility that some of the biological effects of ubiquitylation of H1B are exerted via ubiquitin chains, rather than a single ubiquitIn group.
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