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Nucleic Acids Research Advance Access originally published online on February 16, 2008
Nucleic Acids Research 2008 36(7):2208-2218; doi:10.1093/nar/gkn060
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Nucleic Acids Research, 2008, Vol. 36, No. 7 2208-2218
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Nucleosome formation with the testis-specific histone H3 variant, H3t, by human nucleosome assembly proteins in vitro

Hiroaki Tachiwana1, Akihisa Osakabe1, Hiroshi Kimura2,3 and Hitoshi Kurumizaka1,*

1Laboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, 2Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamada-oka, Suita, Osaka 565-0871 and 3Cell Biology Group, Kansai Advanced Research Center, National Institute of Information and Communications Technology, 588-2 Iwaoka-cho, Nishi-ku, Kobe 651-2492, Japan

*To whom correspondence should be addressed. Tel: +81 3 5286 8189; Fax: +81 3 5292 9211; Email: kurumizaka{at}waseda.jp

Received December 5, 2007. Revised January 22, 2008. Accepted January 30, 2008.

Five non-allelic histone H3 variants, H3.1, H3.2, H3.3, H3t and CENP-A, have been identified in mammals. H3t is robustly expressed in the testis, and thus was assigned as the testis-specific H3 variant. However, recent proteomics and tissue-specific RT-PCR experiments revealed a small amount of H3t expression in somatic cells. In the present study, we purified human H3t as a recombinant protein, and showed that H3t/H4 forms nucleosomes with H2A/H2B by the salt-dialysis method, like the conventional H3.1/H4. We found that H3t/H4 is not efficiently incorporated into the nucleosome by human Nap1 (hNap1), due to its defective H3t/H4 deposition on DNA. In contrast, human Nap2 (hNap2), a paralog of hNap1, promotes nucleosome assembly with H3t/H4. Mutational analyses revealed that the Ala111 residue, which is conserved among H3.1, H3.2 and H3.3, but not in H3t, is the essential residue for the hNap1-mediated nucleosome assembly. These results suggest that H3t may be incorporated into chromatin by a specific chaperone-mediated pathway.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors


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