Association States of Nucleosome Assembly Protein 1 and Its Complexes with Histones
Abstract
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.
Additional Information
© 2005 The American Society for Biochemistry and Molecular Biology, Inc. Received November 26, 2004; Revision received January 10, 2005; First Published on January 31, 2005. The support of Peter Lichter is gratefully acknowledged. We thank Felix Kepert, Malte Wachsmuth, Lutz Ehrhardt, and Borries Demeler for help and Tamas Fischer for valuable discussions. We are grateful to Karolin Luger, Gernot Laengst, and Tom Owen-Hughes for providing plasmid vectors. The project was supported by the Volkswagen Foundation in the program "Junior Research Groups at German Universities." 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.Attached Files
Published - J._Biol._Chem.-2005-Tóth-15690-9.pdf
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- Eprint ID
- 102691
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- CaltechAUTHORS:20200421-091033196
- Volkswagen Foundation
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2020-04-21Created from EPrint's datestamp field
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2021-11-16Created from EPrint's last_modified field