Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor.

@article{Wang2001MethylationOH,
  title={Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor.},
  author={Helen Xuefeng Wang and Zhao Quan Huang and Li Zhan Xia and Qin Fu Feng and Hediye Erdjument-Bromage and Brian D. Strahl and Scott D Briggs and C David Allis and Jeffrey Wong and Paul Tempst and Yan Zhang},
  journal={Science},
  year={2001},
  volume={293 5531},
  pages={853-7}
}
Acetylation of core histone tails plays a fundamental role in transcription regulation. In addition to acetylation, other posttranslational modifications, such as phosphorylation and methylation, occur in core histone tails. Here, we report the purification, molecular identification, and functional characterization of a histone H4-specific methyltransferase PRMT1, a protein arginine methyltransferase. PRMT1 specifically methylates arginine 3 (Arg 3) of H4 in vitro and in vivo. Methylation of… CONTINUE READING
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