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Published Online May 31, 2001
Science DOI: 10.1126/science.1060781

Reports

Submitted on March 16, 2001
Accepted on May 18, 2001

Methylation of Histone H4 at Arginine 3 Facilitates 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 Zhang 1*

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.

Acetylation of core histone tails plays a fundamental role in transcription regulation. In addition to acetylation, other post-translational modifications, such as phosphorylation and methylation, also 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. Importantly, a mutation in the SAM binding site of PRMT1 significantly crippled its nuclear receptor co-activator 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.


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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
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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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