PMID- 20068219
OWN - NLM
STAT- MEDLINE
DCOM- 20100419
LR  - 20211020
IS  - 1528-0020 (Electronic)
IS  - 0006-4971 (Print)
IS  - 0006-4971 (Linking)
VI  - 115
IP  - 10
DP  - 2010 Mar 11
TI  - H4R3 methylation facilitates beta-globin transcription by regulating histone 
      acetyltransferase binding and H3 acetylation.
PG  - 2028-37
LID - 10.1182/blood-2009-07-236059 [doi]
AB  - Histone modifications play an important role in the process of transcription. 
      However, in contrast to lysine methylation, the role of arginine methylation in 
      chromatin structure and transcription has been underexplored. The globin genes 
      are regulated by a highly organized chromatin structure that juxtaposes the locus 
      control region (LCR) with downstream globin genes. We report here that the 
      targeted recruitment of asymmetric dimethyl H4R3 catalyzed by PRMT1 (protein 
      arginine methyltransferase 1) facilitates histone H3 acetylation on Lys9/Lys14. 
      Dimethyl H4R3 provides a binding surface for P300/CBP-associated factor (PCAF) 
      and directly enhances histone H3 acetylation in vitro. We show that these active 
      modifications are essential for efficient interactions between the LCR and the 
      beta(maj)-promoter as well as transcription of the beta-globin gene. Furthermore, 
      knockdown (KD) of PRMT1 by RNA interference in erythroid progenitor cells 
      prevents histone acetylation, enhancer and promoter interaction, and recruitment 
      of transcription complexes to the active beta-globin promoter. Reintroducing rat 
      PRMT1 into the PRMT1 KD MEL cells rescues PRMT1 binding, beta-globin 
      transcription, and erythroid differentiation. Taken together, our data suggest 
      that PRMT1-mediated dimethyl H4R3 facilitates histone acetylation and 
      enhancer/promoter communications, which lead to the efficient recruitment of 
      transcription preinitiation complexes to active promoters.
FAU - Li, Xingguo
AU  - Li X
AD  - Department of Biochemistry and Molecular Biology, University of Florida, PO Box 
      103633, Gainesville, FL 32610, USA.
FAU - Hu, Xin
AU  - Hu X
FAU - Patel, Bhavita
AU  - Patel B
FAU - Zhou, Zhuo
AU  - Zhou Z
FAU - Liang, Shermi
AU  - Liang S
FAU - Ybarra, River
AU  - Ybarra R
FAU - Qiu, Yi
AU  - Qiu Y
FAU - Felsenfeld, Gary
AU  - Felsenfeld G
FAU - Bungert, Jorg
AU  - Bungert J
FAU - Huang, Suming
AU  - Huang S
LA  - eng
GR  - R01 DK052356-15A1/DK/NIDDK NIH HHS/United States
GR  - HL091929/HL/NHLBI NIH HHS/United States
GR  - R01 HL091929/HL/NHLBI NIH HHS/United States
GR  - R01 HL090589/HL/NHLBI NIH HHS/United States
GR  - DK52356/DK/NIDDK NIH HHS/United States
GR  - HL090589/HL/NHLBI NIH HHS/United States
GR  - R01 DK052356/DK/NIDDK NIH HHS/United States
GR  - R01 DK052356-10/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20100112
PL  - United States
TA  - Blood
JT  - Blood
JID - 7603509
RN  - 0 (Histones)
RN  - 0 (beta-Globins)
RN  - 94ZLA3W45F (Arginine)
RN  - EC 2.1.1.- (Histone Methyltransferases)
RN  - EC 2.1.1.319 (Prmt1 protein, mouse)
RN  - EC 2.1.1.319 (Protein-Arginine N-Methyltransferases)
RN  - EC 2.1.1.43 (Histone-Lysine N-Methyltransferase)
RN  - EC 2.3.1.48 (Histone Acetyltransferases)
SB  - IM
MH  - Acetylation
MH  - Animals
MH  - Arginine/metabolism
MH  - Cells, Cultured
MH  - Embryo, Mammalian
MH  - Gene Expression Regulation, Developmental/physiology
MH  - Histone Acetyltransferases/*metabolism/physiology
MH  - Histone Methyltransferases
MH  - Histone-Lysine N-Methyltransferase/metabolism/*physiology
MH  - Histones/*metabolism/physiology
MH  - Methylation
MH  - Mice
MH  - Protein Binding/physiology
MH  - Protein-Arginine N-Methyltransferases/antagonists & 
      inhibitors/genetics/metabolism/physiology
MH  - Transcription, Genetic
MH  - beta-Globins/*genetics/metabolism
PMC - PMC2837319
EDAT- 2010/01/14 06:00
MHDA- 2010/04/20 06:00
PMCR- 2011/03/11
CRDT- 2010/01/14 06:00
PHST- 2010/01/14 06:00 [entrez]
PHST- 2010/01/14 06:00 [pubmed]
PHST- 2010/04/20 06:00 [medline]
PHST- 2011/03/11 00:00 [pmc-release]
AID - S0006-4971(20)56672-X [pii]
AID - 2009/236059 [pii]
AID - 10.1182/blood-2009-07-236059 [doi]
PST - ppublish
SO  - Blood. 2010 Mar 11;115(10):2028-37. doi: 10.1182/blood-2009-07-236059. Epub 2010 
      Jan 12.