PMID- 17227884
OWN - NLM
STAT- MEDLINE
DCOM- 20070507
LR  - 20161124
IS  - 0888-8809 (Print)
IS  - 0888-8809 (Linking)
VI  - 21
IP  - 4
DP  - 2007 Apr
TI  - Dynamic histone acetylation/deacetylation with progesterone receptor-mediated 
      transcription.
PG  - 843-56
AB  - Histone acetylation is a highly dynamic posttranslational modification that plays 
      an important role in gene expression. Previous work showed that promoter histone 
      deacetylation is accompanied by progesterone receptor (PR)-mediated activation of 
      the mouse mammary tumor virus (MMTV) promoter. We investigated the role of this 
      deacetylation and found that this histone deacetylation is not a singular event. 
      In fact, histone acetylation at the MMTV promoter is highly dynamic, with an 
      initial increase in acetylation followed by an eventual net deacetylation of 
      histone H4. The timing of increase in acetylation of H4 coincides with the time 
      at which PR, RNA polymerase II, and histone acetyltransferases cAMP response 
      element-binding protein (CREB)-binding protein and p300 are recruited to the MMTV 
      promoter. The timing in which histone H4 deacetylation occurs (after PR and RNA 
      polymerase II recruitment) and the limited effect that trichostatin A and small 
      interfering RNA knockdown of histone deacetylase (HDAC)3 have on MMTV 
      transcription suggests that this deacetylation activity is not required for the 
      initiation of PR-mediated transcription. Interestingly, two HDACs, HDAC1 and 
      HDAC3, are already present at the MMTV before transcription activation. HDAC 
      association at the MMTV promoter fluctuates during the hormone treatment. In 
      particular, HDAC3 is temporarily undetected at the MMTV promoter within minutes 
      after hormone treatment when the histone H4 acetylation increases but returns to 
      the promoter near the time when histone acetylation levels start to decline. 
      These results demonstrate the dynamic nature of coactivator/corepressor-promoter 
      association and histone modifications such as acetylation during a transcription 
      activation event.
FAU - Aoyagi, Sayura
AU  - Aoyagi S
AD  - Chromatin and Gene Expression Section, Laboratory of Molecular Carcinogenesis, 
      National Institute of Environmental Health Sciences, 111 Alexander Drive, P.O. 
      Box 12233 (MD D4-01), Research Triangle Park, North Carolina 27709, USA.
FAU - Archer, Trevor K
AU  - Archer TK
LA  - eng
GR  - Intramural NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, N.I.H., Intramural
DEP - 20070116
PL  - United States
TA  - Mol Endocrinol
JT  - Molecular endocrinology (Baltimore, Md.)
JID - 8801431
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Histones)
RN  - 0 (Receptors, Progesterone)
RN  - 0 (Transcription Factors)
RN  - EC 2.3.1.48 (CREB-Binding Protein)
RN  - EC 2.3.1.48 (CREBBP protein, human)
RN  - EC 2.3.1.48 (Histone Acetyltransferases)
RN  - EC 2.3.1.48 (p300-CBP Transcription Factors)
RN  - EC 2.3.1.48 (p300-CBP-associated factor)
RN  - EC 2.7.7.- (RNA Polymerase II)
RN  - EC 3.5.1.98 (HDAC1 protein, human)
RN  - EC 3.5.1.98 (Histone Deacetylase 1)
RN  - EC 3.5.1.98 (Histone Deacetylases)
RN  - EC 3.5.1.98 (histone deacetylase 3)
RN  - K3Z4F929H6 (Lysine)
SB  - IM
MH  - Acetylation
MH  - CREB-Binding Protein
MH  - Cell Cycle Proteins
MH  - Cell Line, Tumor
MH  - Chromatin Immunoprecipitation
MH  - Histone Acetyltransferases
MH  - Histone Deacetylase 1
MH  - Histone Deacetylases/metabolism
MH  - Histones/genetics/*metabolism
MH  - Humans
MH  - Lysine/genetics/metabolism
MH  - Mammary Tumor Virus, Mouse/genetics
MH  - Promoter Regions, Genetic/genetics
MH  - Protein Processing, Post-Translational
MH  - RNA Polymerase II/metabolism
MH  - Receptors, Progesterone/*metabolism
MH  - Transcription Factors
MH  - Transcription, Genetic
MH  - *Transcriptional Activation
MH  - p300-CBP Transcription Factors
EDAT- 2007/01/18 09:00
MHDA- 2007/05/08 09:00
CRDT- 2007/01/18 09:00
PHST- 2007/01/18 09:00 [pubmed]
PHST- 2007/05/08 09:00 [medline]
PHST- 2007/01/18 09:00 [entrez]
AID - me.2006-0244 [pii]
AID - 10.1210/me.2006-0244 [doi]
PST - ppublish
SO  - Mol Endocrinol. 2007 Apr;21(4):843-56. doi: 10.1210/me.2006-0244. Epub 2007 Jan 
      16.