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Originally published In Press as doi:10.1074/jbc.M411347200 on October 30, 2004

J. Biol. Chem., Vol. 280, Issue 3, 1817-1825, January 21, 2005
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Nucleosome Assembly Protein 1 Exchanges Histone H2A-H2B Dimers and Assists Nucleosome Sliding*{boxs}

Young-Jun Park, Jayanth V. Chodaparambil, Yunhe Bao, Steven J. McBryant, and Karolin Luger{ddagger}

From the Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523-1870

Eukaryotic chromatin is highly dynamic and turns over rapidly even in the absence of DNA replication. Here we show that the acidic histone chaperone nucleosome assembly protein 1 (NAP-1) from yeast reversibly removes and replaces histone protein dimer H2A-H2B or histone variant dimers from assembled nucleosomes, resulting in active histone exchange. Transient removal of H2A-H2B dimers facilitates nucleosome sliding along the DNA to a thermodynamically favorable position. Histone exchange as well as nucleosome sliding is independent of ATP and relies on the presence of the C-terminal acidic domain of yeast NAP-1, even though this region is not required for histone binding and chromatin assembly. Our results suggest a novel role for NAP-1 (and perhaps other acidic histone chaperones) in mediating chromatin fluidity by incorporating histone variants and assisting nucleosome sliding. NAP-1 may function either untargeted (if acting alone) or may be targeted to specific regions within the genome through interactions with additional factors.

Received for publication, October 5, 2004 , and in revised form, October 27, 2004.

* This work was supported by National Institutes of Health Grants GM561909 and GM067777. 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.

{boxs} The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. 1.

{ddagger} To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, Colorado State University, 316 MRB, Fort Collins, CO 80523-1870. Tel.: 970-491-6405; Fax: 970-491-0494; E-mail: kluger{at}lamar.colostate.edu.


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