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J. Biol. Chem., Vol. 281, Issue 39, 28636-28647, September 29, 2006

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Human ACF1 Alters the Remodeling Strategy of SNF2h^*

From the Department of Molecular Biology, Massachusetts General Hospital, and the Department of Genetics, Harvard Medical School, Boston, Massachusetts 02114

The human ACF chromatin-remodeling complex (hACF) contains the ATPase motor protein SNF2h and the non-catalytic hACF1 subunit. Here, we have compared the ability of SNF2h and a reconstituted hACF complex containing both SNF2h and hACF1 to remodel a series of nucleosomes containing different lengths of DNA overhang. Both SNF2h and hACF functioned in a manner consistent with sliding a canonical nucleosome. However, the non-catalytic subunit, hACF1, altered the remodeling properties of SNF2h by changing the nature of the requirement for a DNA overhang in the nucleosomal substrate and altering the DNA accessibility profile of the remodeled products. Surprisingly, addition of hACF1 to SNF2h increased the amount of DNA overhang needed to observe measurable amounts of DNA accessibility, but decreased the amount of overhang needed for a measurable binding interaction. We propose that these hACF1 functions might contribute to making the hACF complex more efficient at nucleosome spacing compared with SNF2h. In contrast, the SWI/SNF complex and its ATPase subunit BRG1 generated DNA accessibility profiles that were similar to each other, but different significantly from those of hACF and SNF2h. Thus, we observed divergent remodeling behaviors in these two remodeling families and found that the manner in which hACF1 alters the remodeling behavior of the ATPase is not shared by SWI/SNF subunits.

Received for publication, March 30, 2006 , and in revised form, June 30, 2006.

^* This work was supported by grants from the National Institutes of Health (GM48405 to R. E. K.) and from the National Science Foundation (to X. H.) and by NCI Grant CA-093660 from the National Institutes of Health (to H.-Y. F.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. 1 and 2.

¹ Present address: Dept. of Biochemistry and Biophysics, University of California, San Francisco, CA 94143.

² To whom correspondence should be addressed: Dept. of Molecular Biology, Simches Research Bldg., CPZN7811B, Massachusetts General Hospital, 185 Cambridge St., Boston, MA 02114. Tel.: 617-726-5990; Fax: 617-726-5949; E-mail: kingston{at}molbio.mgh.harvard.edu.

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This article has been cited by other articles:

				K. Bouazoune, T. B. Miranda, P. A. Jones, and R. E. Kingston Analysis of individual remodeled nucleosomes reveals decreased histone-DNA contacts created by hSWI/SNF Nucleic Acids Res., June 30, 2009; (2009) gkp524v1. [Abstract] [Full Text] [PDF]