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Nucleic Acids Research Advance Access published online on November 11, 2009

Nucleic Acids Research, doi:10.1093/nar/gkp1030
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© The Author(s) 2009. Published by Oxford University Press.
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.


Gene Regulation, Chromatin and Epigenetics

Divergent human remodeling complexes remove nucleosomes from strong positioning sequences

Chuong D. Pham, Xi He and Gavin R. Schnitzler*

Molecular Cardiology Research Institute, Tufts Medical Center, Boston, MA 02111, USA

*To whom correspondence should be addressed. Tel: +1 617 636 0615; Fax: +1 617 636 1444; Email: gschnitzler{at}tuftsmedicalcenter.org

Received August 21, 2009. Revised October 7, 2009. Accepted October 21, 2009.

Nucleosome positioning plays a major role in controlling the accessibility of DNA to transcription factors and other nuclear processes. Nucleosome positions after assembly are at least partially determined by the relative affinity of DNA sequences for the histone octamer. Nucleosomes can be moved, however, by a class of ATP dependent chromatin remodeling complexes. We recently showed that the human SWI/SNF remodeling complex moves nucleosomes in a sequence specific manner, away from nucleosome positioning sequences (NPSes). Here, we compare the repositioning specificity of five remodelers of diverse biological functions (hSWI/SNF, the SNF2h ATPase and the hACF, CHRAC and WICH complexes than each contain SNF2h) on 5S rDNA, MMTV and 601 NPS polynucleosomal templates. We find that all five remodelers act similarly to reduce nucleosome occupancy over the strongest NPSes, an effect that could directly contribute to the function of WICH in activating 5S rDNA transcription. While some differences were observed between complexes, all five remodelers were found to result in surprisingly similar nucleosome distributions. This suggests that remodeling complexes may share a conserved repositioning specificity, and that their divergent biological functions may largely arise from other properties conferred by complex-specific subunits.


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