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Molecular and Cellular Biology, September 2003, p. 6672-6684, Vol. 23, No. 18
0270-7306/03/$08.00+0 DOI: 10.1128/MCB.23.18.6672-6684.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Involvement of Nucleocytoplasmic Shuttling of Yeast Nap1 in Mitotic Progression
Mary Miyaji-Yamaguchi,1,
Kohsuke Kato,1,2 Ryosuke Nakano,2,
Tomohiro Akashi,3 Akihiko Kikuchi,3 and Kyosuke Nagata1*
Department of Infection Biology, Institute of Basic Medical Sciences, University of Tsukuba, Tsukuba 305-8575,1
Department of Biological Information, Tokyo Institute of Technology, Yokohama 226-8501,2
Department of Medical Mycology, Nagoya University, Nagoya 466-8550, Japan3
Received 5 May 2003/
Accepted 24 June 2003
Nucleosome assembly protein 1 (Nap1) is widely conserved from yeasts to humans and facilitates nucleosome formation in vitro as a histone chaperone. Nap1 is generally localized in the cytoplasm, except that subcellular localization of Drosophila melanogaster Nap1 is dynamically regulated between the cytoplasm and nucleus during early development. The cytoplasmic localization of Nap1 is seemingly incompatible with the proposed role of Nap1 in nucleosome formation, which should occur in the nucleus. Here, we have examined the roles of a putative nuclear export signal (NES) sequence in yeast Nap1 (yNap1). yNap1 mutants lacking the NES-like sequence were localized predominantly in the nucleus. Deletion of NAP1 in cells harboring a single mitotic cyclin gene is known to cause mitotic delay and temperature-sensitive growth. A wild-type NAP1 complemented these phenotypes while nap1 mutant genes lacking the NES-like sequence or carboxy-terminal region did not. These and other results suggest that yNap1 is a nucleocytoplasmic shuttling protein and that its shuttling is important for yNap1 function during mitotic progression. This study also provides a possible explanation for Nap1's involvement in nucleosome assembly and/or remodeling in the nucleus.
* Corresponding author. Mailing address: Department of Infection Biology, Institute of Basic Medical Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba 305-8575, Japan. Phone: 81-298-53-3233. Fax: 81-298-53-3134. E-mail:
knagata{at}md.tsukuba.ac.jp.
Present address: Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, Kanagawa 199-0195, Japan.
Present address: Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Tokyo 194-8533, Japan.
Molecular and Cellular Biology, September 2003, p. 6672-6684, Vol. 23, No. 18
0022-538X/03/$08.00+0 DOI: 10.1128/MCB.23.18.6672-6684.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
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