NuA4 links methylation of histone H3 lysines 4 and 36 to acetylation of histones H4 and H3.

@article{Ginsburg2014NuA4LM,
  title={NuA4 links methylation of histone H3 lysines 4 and 36 to acetylation of histones H4 and H3.},
  author={Daniel S. Ginsburg and Timi Elvuchio Anlembom and Jianing Wang and Sanket R Patel and Bing Li and Alan G Hinnebusch},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 47},
  pages={32656-70}
}
Cotranscriptional methylation of histone H3 lysines 4 and 36 by Set1 and Set2, respectively, stimulates interaction between nucleosomes and histone deacetylase complexes to block cryptic transcription in budding yeast. We previously showed that loss of all H3K4 and H3K36 methylation in a set1Δset2Δ mutant reduces interaction between native nucleosomes and the NuA4 lysine acetyltransferase (KAT) complex. We now provide evidence that NuA4 preferentially binds H3 tails mono- and dimethylated on… CONTINUE READING
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