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Nucleic Acids Research Advance Access originally published online on March 28, 2007
Nucleic Acids Research 2007 35(7):2403-2412; doi:10.1093/nar/gkm157
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Nucleic Acids Research, 2007, Vol. 35, No. 7 2403-2412
© 2007 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

Analysis of the role of Aurora B on the chromosomal targeting of condensin I

Ai Takemoto1,2,3,4, Akiko Murayama1, Miyuki Katano1, Takeshi Urano5, Koichi Furukawa5, Shigeyuki Yokoyama3,4, Junn Yanagisawa1, Fumio Hanaoka2,6 and Keiji Kimura1,2,*

1Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba Science City, Ibaraki 305-8572, Japan, 2Cellular Physiology Laboratory, Discovery Research Institute, RIKEN and SORST, Japan Science and Technology Agency, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan, 3Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan, 4RIKEN Genomic Sciences Center, 1-7-22, Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan, 5Department of Biochemistry II, Nagoya University Graduate School of Medicine, Showa-ku, Nagoya, Japan and 6Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamada-oka, Suita, Osaka 565-0871, Japan

*To whom correspondence should be addressed. Tel: +81-29-853-6632; Fax: +81-29-853-4605; Email: kekimura{at}sakura.cc.tsukuba.ac.jp

Received January 23, 2007. Revised March 1, 2007. Accepted March 1, 2007.

During mitosis, chromosome condensation takes place, which entails the conversion of interphase chromatin into compacted mitotic chromosomes. Condensin I is a five-subunit protein complex that plays a central role in this process. Condensin I is targeted to chromosomes in a mitosis-specific manner, which is regulated by phosphorylation by mitotic kinases. Phosphorylation of histone H3 at serine 10 (Ser10) occurs during mitosis and its physiological role is a longstanding question. We examined the function of Aurora B, a kinase that phosphorylates Ser10, in the chromosomal binding of condensin I and mitotic chromosome condensation, using an in vitro system derived from Xenopus egg extract. Aurora B depletion from a mitotic egg extract resulted in the loss of H3 phosphorylation, accompanied with a 50% reduction of chromosomal targeting of condensin I. Alternatively, a portion of condensin I was bound to sperm chromatin, and chromosome-like structures were assembled when okadaic acid (OA) was supplemented in an interphase extract that lacks Cdc2 activity. However, chromosomal targeting of condensin I was abolished when Aurora B was depleted from the OA-treated interphase extract. From these results, it is suggested that Aurora B-dependent and Cdc2-independent pathways of the chromosomal targeting of condensin I are present.


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