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Molecular and Cellular Biology, December 2005, p. 10639-10651, Vol. 25, No. 23
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.23.10639-10651.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Assembly and Disassembly of Nucleosome Core Particles Containing Histone Variants by Human Nucleosome Assembly Protein I{dagger}

Mitsuru Okuwaki,1* Kohsuke Kato,1 Hideto Shimahara,2 Shin-ichi Tate,3 and Kyosuke Nagata1

Graduate School of Comprehensive Human Sciences and Institute of Basic Medical Sciences, University of Tsukuba, 1-1-1 Tennohdai, Tsukuba 305-8575, Japan,1 Center for New Materials, Japan Advanced Institute of Science and Technology, 1-1 Asahidai, Nomi-shi 923-1292, Japan,2 Department of Structural Biology, Biomolecular Engineering Research Institute, 6-2-3 Furuedai, Suita 565-0874, Japan3

Received 29 August 2005/ Accepted 12 September 2005

Histone variants play important roles in the maintenance and regulation of the chromatin structure. In order to characterize the biochemical properties of the chromatin structure containing histone variants, we investigated the dynamic status of nucleosome core particles (NCPs) that were assembled with recombinant histones. We found that in the presence of nucleosome assembly protein I (NAP-I), a histone chaperone, H2A-Barr body deficient (H2A.Bbd) confers the most flexible nucleosome structure among the mammalian histone H2A variants known thus far. NAP-I mediated the efficient assembly and disassembly of the H2A.Bbd-H2B dimers from NCPs. This reaction was accomplished more efficiently when the NCPs contained H3.3, a histone H3 variant known to be localized in the active chromatin, than when the NCPs contained the canonical H3. These observations indicate that the histone variants H2A.Bbd and H3.3 are involved in the formation and maintenance of the active chromatin structure. We also observed that acidic histone binding proteins, TAF-I/SET and B23.1, demonstrated dimer assembly and disassembly activity, but the efficiency of their activity was considerably lower than that of NAP-I. Thus, both the acidic nature of NAP-I and its other functional structure(s) may be essential to mediate the assembly and disassembly of the dimers in NCPs.

* Corresponding author. Mailing address: Graduate School of Comprehensive Human Sciences and Institute of Basic Medical Sciences, University of Tsukuba, 1-1-1 Tennohdai, Tsukuba 305-8575, Japan. Phone: 81-29-853-3472. Fax: 81-29-853-3233. E-mail: mokuwaki{at}md.tsukuba.ac.jp.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

Molecular and Cellular Biology, December 2005, p. 10639-10651, Vol. 25, No. 23
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.23.10639-10651.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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