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Mol Cell Biol
2006 Feb 01;263:1156-64. doi: 10.1128/MCB.26.3.1156-1164.2006.
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Mechanism of polymerase II transcription repression by the histone variant macroH2A.
Doyen CM, An W, Angelov D, Bondarenko V, Mietton F, Studitsky VM, Hamiche A, Roeder RG, Bouvet P, Dimitrov S.
???displayArticle.abstract??? macroH2A (mH2A) is an unusual histone variant consisting of a histone H2A-like domain fused to a large nonhistone region. In this work, we show that histone mH2A represses p300- and Gal4-VP16-dependent polymerase II transcription, and we have dissected the mechanism by which this repression is realized. The repressive effect of mH2A is observed at the level of initiation but not at elongation of transcription, and mH2A interferes with p300-dependent histone acetylation. The nonhistone region of mH2A is responsible for both the repression of initiation of transcription and the inhibition of histone acetylation. In addition, the presence of this domain of mH2A within the nucleosome is able to block nucleosome remodeling and sliding of the histone octamer to neighboring DNA segments by the remodelers SWI/SNF and ACF. These data unambiguously identify mH2A as a strong transcriptional repressor and show that the repressive effect of mH2A is realized on at least two different transcription activation chromatin-dependent pathways: histone acetylation and nucleosome remodeling.
Allen,
The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A.
2003, Pubmed
Allen,
The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A.
2003,
Pubmed An,
Direct association of p300 with unmodified H3 and H4 N termini modulates p300-dependent acetylation and transcription of nucleosomal templates.
2003,
Pubmed
,
Xenbase An,
Selective requirements for histone H3 and H4 N termini in p300-dependent transcriptional activation from chromatin.
2002,
Pubmed
,
Xenbase Angelov,
The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling.
2003,
Pubmed Angelov,
SWI/SNF remodeling and p300-dependent transcription of histone variant H2ABbd nucleosomal arrays.
2004,
Pubmed
,
Xenbase Arents,
The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix.
1991,
Pubmed Bassing,
Histone H2AX: a dosage-dependent suppressor of oncogenic translocations and tumors.
2003,
Pubmed Celeste,
H2AX haploinsufficiency modifies genomic stability and tumor susceptibility.
2003,
Pubmed Chadwick,
A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome.
2001,
Pubmed Chadwick,
Histone variant macroH2A contains two distinct macrochromatin domains capable of directing macroH2A to the inactive X chromosome.
2001,
Pubmed Chakravarthy,
Structural characterization of the histone variant macroH2A.
2005,
Pubmed
,
Xenbase Costanzi,
Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals.
1998,
Pubmed Costanzi,
MACROH2A2, a new member of the MARCOH2A core histone family.
2001,
Pubmed Côté,
Stimulation of GAL4 derivative binding to nucleosomal DNA by the yeast SWI/SNF complex.
1994,
Pubmed Dhillon,
A histone variant, Htz1p, and a Sir1p-like protein, Esc2p, mediate silencing at HMR.
2000,
Pubmed Gautier,
Histone variant H2ABbd confers lower stability to the nucleosome.
2004,
Pubmed Hayes,
In vitro reconstitution and analysis of mononucleosomes containing defined DNAs and proteins.
1997,
Pubmed
,
Xenbase Ito,
ACF consists of two subunits, Acf1 and ISWI, that function cooperatively in the ATP-dependent catalysis of chromatin assembly.
1999,
Pubmed Kagalwala,
Topography of the ISW2-nucleosome complex: insights into nucleosome spacing and chromatin remodeling.
2004,
Pubmed Karras,
The macro domain is an ADP-ribose binding module.
2005,
Pubmed Kireeva,
Nucleosome remodeling induced by RNA polymerase II: loss of the H2A/H2B dimer during transcription.
2002,
Pubmed Kundu,
Activator-dependent transcription from chromatin in vitro involving targeted histone acetylation by p300.
2000,
Pubmed Kustatscher,
Splicing regulates NAD metabolite binding to histone macroH2A.
2005,
Pubmed Ladurner,
Inactivating chromosomes: a macro domain that minimizes transcription.
2003,
Pubmed Luger,
Crystal structure of the nucleosome core particle at 2.8 A resolution.
1997,
Pubmed Luger,
Expression and purification of recombinant histones and nucleosome reconstitution.
1999,
Pubmed Mermoud,
Histone macroH2A1.2 relocates to the inactive X chromosome after initiation and propagation of X-inactivation.
1999,
Pubmed Mizuguchi,
ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex.
2004,
Pubmed Pehrson,
MacroH2A, a core histone containing a large nonhistone region.
1992,
Pubmed Perche,
Higher concentrations of histone macroH2A in the Barr body are correlated with higher nucleosome density.
2000,
Pubmed Rangasamy,
RNA interference demonstrates a novel role for H2A.Z in chromosome segregation.
2004,
Pubmed Santisteban,
Histone H2A.Z regulats transcription and is partially redundant with nucleosome remodeling complexes.
2000,
Pubmed Thåström,
Sequence motifs and free energies of selected natural and non-natural nucleosome positioning DNA sequences.
1999,
Pubmed
