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Originally published in Science Express on 31 May 2001
Science 3 August 2001:
Vol. 293. no. 5531, pp. 853 - 857
DOI: 10.1126/science.1060781
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Reports

Methylation of Histone H4 at Arginine 3 Facilitating Transcriptional Activation by Nuclear Hormone Receptor

Hengbin Wang,1 Zhi-Qing Huang,2 Li Xia,1 Qin Feng,1 Hediye Erdjument-Bromage,3 Brian D. Strahl,4 Scott D. Briggs,4 C. David Allis,4 Jiemin Wong,2 Paul Tempst,3 Yi Zhang1*

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 Arg 3 by PRMT1 facilitates subsequent acetylation of H4 tails by p300. However, acetylation of H4 inhibits its methylation by PRMT1. Most important, a mutation in the S-adenosyl-L-methionine-binding site of PRMT1 substantially crippled its nuclear receptor coactivator activity. Our finding reveals Arg 3 of H4 as a novel methylation site by PRMT1 and indicates that Arg 3 methylation plays an important role in transcriptional regulation.

1 Department of Biochemistry and Biophysics, Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7295, USA.
2 Department of Molecular and Cellular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
3 Molecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10021, USA.
4 Department of Biochemistry and Molecular Genetics, University of Virginia Health Science Center, Charlottesville, VA 22908, USA.
*   To whom correspondence should be addressed. E-mail: yi_zhang{at}med.unc.edu

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Purification and Identification of a Novel Complex Which Is Involved in Androgen Receptor-Dependent Transcription.
K. Hosohata, P. Li, Y. Hosohata, J. Qin, R. G. Roeder, and Z. Wang (2003)
Mol. Cell. Biol. 23, 7019-7029
   Abstract »    Full Text »    PDF »
Chromatin of the Barr body: histone and non-histone proteins associated with or excluded from the inactive X chromosome.
B. P. Chadwick and H. F. Willard (2003)
Hum. Mol. Genet. 12, 2167-2178
   Abstract »    Full Text »    PDF »
The Interplay between the Glucocorticoid Receptor and Nuclear Factor-{kappa}B or Activator Protein-1: Molecular Mechanisms for Gene Repression.
K. De Bosscher, W. Vanden Berghe, and G. Haegeman (2003)
Endocr. Rev. 24, 488-522
   Abstract »    Full Text »    PDF »
Transcriptional Elongation by RNA Polymerase II and Histone Methylation.
M. Gerber and A. Shilatifard (2003)
J. Biol. Chem. 278, 26303-26306
   Abstract »    Full Text »    PDF »
BRCA2 cooperates with histone acetyltransferases in androgen receptor-mediated transcription.
S. Shin and I. M. Verma (2003)
PNAS 100, 7201-7206
   Abstract »    Full Text »    PDF »
An epigenetic road map for histone lysine methylation.
M. Lachner, R. J. O'Sullivan, and T. Jenuwein (2003)
J. Cell Sci. 116, 2117-2124
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CBP Recruitment and Histone Acetylation in Differential Gene Induction by Glucocorticoids and Progestins.
J. R. Lambert and S. K. Nordeen (2003)
Mol. Endocrinol. 17, 1085-1094
   Abstract »    Full Text »    PDF »
Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice.
N. Yadav, J. Lee, J. Kim, J. Shen, M. C.-T. Hu, C. M. Aldaz, and M. T. Bedford (2003)
PNAS 100, 6464-6468
   Abstract »    Full Text »    PDF »
The Nonessential H2A N-Terminal Tail Can Function as an Essential Charge Patch on the H2A.Z Variant N-Terminal Tail.
Q. Ren and M. A. Gorovsky (2003)
Mol. Cell. Biol. 23, 2778-2789
   Abstract »    Full Text »    PDF »
Targeted recruitment of a histone H4-specific methyltransferase by the transcription factor YY1.
N. Rezai-Zadeh, X. Zhang, F. Namour, G. Fejer, Y.-D. Wen, Y.-L. Yao, I. Gyory, K. Wright, and E. Seto (2003)
Genes & Dev. 17, 1019-1029
   Abstract »    Full Text »    PDF »
The Drosophila Trithorax protein is a coactivator required to prevent re-establishment of Polycomb silencing.
S. Poux, B. Horard, C. J. A. Sigrist, and V. Pirrotta (2003)
Development 129, 2483-2493
   Abstract »    Full Text »    PDF »
Sam68 RNA Binding Protein Is an In Vivo Substrate for Protein Arginine N-Methyltransferase 1.
J. Cote, F.-M. Boisvert, M.-C. Boulanger, M. T. Bedford, and S. Richard (2003)
Mol. Biol. Cell 14, 274-287
   Abstract »    Full Text »
Symmetrical dimethylarginine methylation is required for the localization of SMN in Cajal bodies and pre-mRNA splicing.
F.-M. Boisvert, J. Cote, M.-C. Boulanger, P. Cleroux, F. Bachand, C. Autexier, and S. Richard (2002)
J. Cell Biol. 159, 957-969
   Abstract »    Full Text »    PDF »
Characterization of the Two Coactivator-interacting Surfaces of the Androgen Receptor and Their Relative Role in Transcriptional Control*.
V. Christiaens, C. L. Bevan, L. Callewaert, A. Haelens, G. Verrijdt, W. Rombauts, and F. Claessens (2002)
J. Biol. Chem. 277, 49230-49237
   Abstract »    Full Text »    PDF »
Nuclear Localization of Peptidylarginine Deiminase V and Histone Deimination in Granulocytes.
K. Nakashima, T. Hagiwara, and M. Yamada (2002)
J. Biol. Chem. 277, 49562-49568
   Abstract »    Full Text »    PDF »


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