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Originally published In Press as doi:10.1074/jbc.M305636200 on August 19, 2003

J. Biol. Chem., Vol. 278, Issue 45, 44574-44583, November 7, 2003
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Preferential Binding of the Histone (H3-H4)2 Tetramer by NAP1 Is Mediated by the Amino-terminal Histone Tails*

Steven J. McBryant, Young-Jun Park, Stephanie M. Abernathy, Paul J. Laybourn, Jennifer K. Nyborg, and Karolin Luger{ddagger}

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

The yeast nucleosome assembly protein 1 (yNAP1) participates in many diverse activities, such as the assembly of newly synthesized DNA into chromatin and the rearrangement of nucleosomes during transcriptional activation. yNAP1 does not require ATP hydrolysis to perform these functions and is a valuable tool for in vitro chromatin assembly. Using recombinant histone complexes, we show that yNAP1 has a preference for binding the (H3-H4)2 tetramer over the (H2A-H2B) dimer. We find that the loss of the histone tails abrogates this preference for H3 and H4, and we demonstrate a direct interaction between yNAP1 and the amino-terminal tails of H3 and H4. yNAP1 binds to one histone fold domain, thus specifying the stoichiometry of the complexes formed with the histone dimer and tetramer. Finally, we provide evidence that the acidic carboxyl-terminal region of yNAP1, although dispensable for nucleosome assembly in vitro, contributes to binding via structure-independent electrostatic interactions. Our results are consistent with recent mechanistic investigations of NAP1 and expand our understanding of the histone chaperone family of assembly factors.

Received for publication, May 29, 2003 , and in revised form, August 12, 2003.

* This study was supported by Grant CA80002 from the NCI, National Institutes of Health (to J. K. N.) and by Grant GM067777 from the NIGMS, National Institutes of Health (to K. L.). 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.

{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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