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J. Biol. Chem., Vol. 280, Issue 16, 15690-15699, April 22, 2005

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Association States of Nucleosome Assembly Protein 1 and Its Complexes with Histones^*

Katalin Fejes Tóth, Jacek Mazurkiewicz, and Karsten Rippe¶

From the Kirchhoff-Institut für Physik, AG Molekulare Biophysik, Ruprecht-Karls-Universität Heidelberg, Im Neuenheimer Feld 227 and the Deutsches Krebsforschungszentrum, Abt. Molekulare Genetik (B060), Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany

The histone chaperone NAP1 is a carrier of histones during nuclear import, nucleosome assembly, and chromatin remodeling. Analytical ultracentrifugation was used to determine the association states of NAP1 alone and in complexes with core histones. In addition, the concentration dependence of the association was quantified by determining the equilibrium dissociation constant between different NAP1 species. At physiological protein and salt concentrations the prevalent species were the NAP1 dimer and octamer. These were also the association states found to interact with histones in a stoichiometry of one NAP1 monomer per histone. Based on these results a model for a cell cycle-dependent shift of the NAP1 dimer-octamer equilibrium is proposed that reflects different biological functions of NAP1.

Received for publication, November 26, 2004 , and in revised form, January 10, 2005.

^* 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.

^¶ To whom correspondence should be addressed. Tel.: 49-6221-54-9270; Fax: 49-6221-54-9112; E-mail: Karsten.Rippe{at}kip.uni-heidelberg.de.

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