Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1

@article{Strahl2001MethylationOH,
  title={Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1},
  author={Brian D. Strahl and Scott D Briggs and Cynthia J. Brame and Jennifer A. Caldwell and Stephen S Koh and Han Ma and Richard G. Cook and Jeffrey Shabanowitz and Donald F. Hunt and Michael R Stallcup and C David Allis},
  journal={Current Biology},
  year={2001},
  volume={11},
  pages={996-1000}
}
Posttranslational modifications of histone amino termini play an important role in modulating chromatin structure and function. Lysine methylation of histones has been well documented, and recently this modification has been linked to cellular processes involving gene transcription and heterochromatin assembly. However, the existence of arginine methylation on histones has remained unclear. Recent discoveries of protein arginine methyltransferases, CARM1 and PRMT1, as transcriptional… CONTINUE READING

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