Peterson CLChromatin remodeling enzymes: taming the machines. Third in review series on chromatin dynamics. EMBO Rep. 3: 319-322

Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
EMBO Reports (Impact Factor: 9.06). 05/2002; 3(4):319-22. DOI: 10.1093/embo-reports/kvf075
Source: PubMed


Members of the ATP-dependent family of chromatin remodeling enzymes play key roles in the regulation of transcription, development, DNA repair and cell cycle. Each of these enzymes are multi-subunit assemblies that hydrolyze thousands of molecules of ATP in order to change nucleosome positions, disrupt DNA-histone interactions and perhaps destabilize chromatin folding. Here I review recent studies that suggest these potent machines can be 'tamed' by one of several mechanisms: targeting their activity to localized regions, blocking their chromatin binding activity or inhibiting their remodeling activity.

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Available from: Craig L Peterson, Sep 17, 2014
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    • "The SWI/SNF chromatin-remodeling complex contributes to the regulation of gene expression by either transcriptional activation or transcriptional repression depending on genetic context and cellular environment (Muchardt and Yaniv, 2001; Klochendler-Yeivin et al., 2002). Although the SWI/SNF complex consists of multiple subunits, the catalytic subunits, BRG1 and BRM, play a key role in chromatin remodeling by utilizing ATP hydrolysis (Peterson, 2002; Narlikar et al., 2002; Roberts and Orkin, 2004). To establish the role of the SWI/SNF complex in the transcriptional regulation of the MMTV-LTR, we carried out transcription reporter assays in the human adrenal carcinoma cell line (SW13). "
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    ABSTRACT: Brahma (BRM) and Brahma-related gene 1 (BRG1) are the ATP-dependent catalytic subunits of the SWI/SNF family of chromatin-remodeling complexes. These complexes are involved in essential processes such as cell cycle, growth, differentiation, and cancer. Using imaging approaches in a cell line that harbors tandem repeats of stably integrated copies of the steroid responsive MMTV-LTR (mouse mammary tumor virus-long terminal repeat), we show that BRG1 and BRM are recruited to the MMTV promoter in a hormone-dependent manner. The recruitment of BRG1 and BRM resulted in chromatin remodeling and decondensation of the MMTV repeat as demonstrated by an increase in the restriction enzyme accessibility and in the size of DNA fluorescence in situ hybridization (FISH) signals. This chromatin remodeling event was concomitant with an increased occupancy of RNA polymerase II and transcriptional activation at the MMTV promoter. The expression of ATPase-deficient forms of BRG1 (BRG1-K-R) or BRM (BRM-K-R) inhibited the remodeling of local and higher order MMTV chromatin structure and resulted in the attenuation of transcription. In vivo photobleaching experiments provided direct evidence that BRG1, BRG1-K-R, and BRM chromatin-remodeling complexes have distinct kinetic properties on the MMTV array, and they dynamically associate with and dissociate from MMTV chromatin in a manner dependent on hormone and a functional ATPase domain. Our data provide a kinetic and mechanistic basis for the BRG1 and BRM chromatin-remodeling complexes in regulating gene expression at a steroid hormone inducible promoter.
    Preview · Article · Jun 2008 · Molecular biology of the cell
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    • "(E) FACS profile of propidium iodide-treated cells after treatments for cell cycle arrests shown above. Chromatin regulation of OriP J Zhou et al & 2005 European Molecular Biology Organization The EMBO Journal VOL 24 | NO 7 | 2005 1409 Peterson, 2002; Lusser and Kadonaga, 2003; Bowen et al, 2004 "
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    ABSTRACT: Selection and licensing of mammalian DNA replication origins may be regulated by epigenetic changes in chromatin structure. The Epstein-Barr virus (EBV) origin of plasmid replication (OriP) uses the cellular licensing machinery to regulate replication during latent infection of human cells. We found that the minimal replicator sequence of OriP, referred to as the dyad symmetry (DS), is flanked by nucleosomes. These nucleosomes were subject to cell cycle-dependent chromatin remodeling and histone modifications. Restriction enzyme accessibility assay indicated that the DS-bounded nucleosomes were remodeled in late G1. Remarkably, histone H3 acetylation of DS-bounded nucleosomes decreased during late G1, coinciding with nucleosome remodeling and MCM3 loading, and preceding the onset of DNA replication. The ATP-dependent chromatin-remodeling factor SNF2h was also recruited to DS in late G1, and formed a stable complex with HDAC2 at DS. siRNA depletion of SNF2h reduced G1-specific nucleosome remodeling, histone deacetylation, and MCM3 loading at DS. We conclude that an SNF2h-HDAC1/2 complex coordinates G1-specific chromatin remodeling and histone deacetylation with the DNA replication initiation process at OriP.
    Full-text · Article · May 2005 · The EMBO Journal
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    • "The functional state of chromatin is regulated, in part, by histone modifying enzymes and ATPdependent chromatin remodeling enzymes. Members of the latter enzyme class alter the structure of nucleosomes or slide them along DNA in vitro (reviewed in Becker and Horz 2002; Peterson 2002). These enzymes have a catalytic DNA-dependent ATPase subunit, which is similar in sequence to those of the DEAD/DEAH-box class of RNA-dependent ATPases. "
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    ABSTRACT: The conserved histone variant H2A.Z functions in euchromatin to antagonize the spread of heterochromatin. The mechanism by which histone H2A is replaced by H2A.Z in the nucleosome is unknown. We identified a complex containing 13 different polypeptides associated with a soluble pool of H2A.Z in Saccharomyces cerevisiae. This complex was designated SWR1-Com in reference to the Swr1p subunit, a Swi2/Snf2-paralog. Swr1p and six other subunits were found only in SWR1-Com, whereas six other subunits were also found in the NuA4 histone acetyltransferase and/or the Ino80 chromatin remodeling complex. H2A.Z and SWR1 were essential for viability of cells lacking the EAF1 component of NuA4, pointing to a close functional connection between these two complexes. Strikingly, chromatin immunoprecipitation analysis of cells lacking Swr1p, the presumed ATPase of the complex, revealed a profound defect in the deposition of H2A.Z at euchromatic regions that flank the silent mating type cassette HMR and at 12 other chromosomal sites tested. Consistent with a specialized role for Swr1p in H2A.Z deposition, the majority of the genome-wide transcriptional defects seen in swr1Delta cells were also found in htz1Delta cells. These studies revealed a novel role for a member of the ATP-dependent chromatin remodeling enzyme family in determining the region-specific histone subunit composition of chromatin in vivo and controlling the epigenetic state of chromatin. Metazoan orthologs of Swr1p (Drosophila Domino; human SRCAP and p400) may have analogous functions.
    Full-text · Article · Jun 2004 · PLoS Biology
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