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J. Biol. Chem., Vol. 282, Issue 27, 19418-19425, July 6, 2007

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The Dpb4 Subunit of ISW2 Is Anchored to Extranucleosomal DNA^*

From the Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, Illinois 62901-4413

Histone fold proteins Dpb4 and Dls1 are components of the yeast ISW2 chromatin remodeling complex that resemble the smaller subunits of the CHRAC (Chromatin Accessibility Complex) complex found in Drosophila and humans. DNA photoaffinity labeling found that the Dpb4 subunit contacts extranucleosomal DNA 37–53 bp away from the entry/exit site of the nucleosome. Binding of Dpb4 to Isw2 and Itc2, the two largest subunits of ISW2, was found to require Dls1. Even after remodeling and nucleosome movement, Dpb4 tends to remain bound to its original binding site and likely serves as an anchor point for ISW2 on DNA. In vitro, only minor differences can be detected in the nucleosome binding and mobilization properties of ISW2 with or without Dpb4 and Dls1. Changes in the contacts of the largest subunit Itc1 with extranucleosomal DNA have, however, been found upon deletion of the Dpb4 and Dls1 dimer that may affect the nucleosome spacing properties of ISW2.

Received for publication, January 23, 2007 , and in revised form, April 12, 2007.

^* 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.

¹ Current address: The Wistar Institute, 3601 Spruce St., Rm. 201, Philadelphia, PA 19104.

² Current address: Dept. of Molecular Genetics, Section of Cancer Genetics, M. D. Anderson Cancer Center, Houston, TX 77030.

³ To whom correspondence should be addressed. E-mail: bbartholomew{at}siumed.edu.

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				W. Dang and B. Bartholomew Domain Architecture of the Catalytic Subunit in the ISW2-Nucleosome Complex Mol. Cell. Biol., December 1, 2007; 27(23): 8306 - 8317. [Abstract] [Full Text] [PDF]