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Vol. 20, Issue 18, 3986-3995, September 15, 2009

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CENP-H–containing Complex Facilitates Centromere Deposition of CENP-A in Cooperation with FACT and CHD1

Masahiro Okada^*,, Katsuya Okawa, Toshiaki Isobe, and Tatsuo Fukagawa

*Center for Priority Areas, Tokyo Metropolitan University, Hachioji, Tokyo 192-0397, Japan; Department of Chemistry, Graduate School of Sciences and Engineering, Tokyo Metropolitan University, Hachioji, Tokyo 192-0397, Japan; Innovative Drug Research Laboratories, Kyowa Hakko Kirin Co., Ltd., Takasaki, Gumma, 370-1295, Japan; and Department of Molecular Genetics, National Institute of Genetics and The Graduate University for Advanced Studies, Mishima, Shizuoka 411-8540, Japan

Submitted January 22, 2009; Revised July 10, 2009; Accepted July 13, 2009
Monitoring Editor: Wendy Bickmore

InCytes from MBC

Centromere identity is thought to be determined by epigenetic mechanisms. The centromere-specific histone H3 variant CENP-A plays a central role in specifying the locus where the centromere is constructed. However, the precise mechanisms that target CENP-A to centromeric chromatin are poorly understood. Here, we show that facilitates chromatin transcription (FACT) localizes to centromeres in a CENP-H–containing complex-dependent manner. In conditional mutant cell lines for SSRP1, a subunit of FACT, centromere targeting of newly synthesized CENP-A is severely inhibited. The chromatin remodeling factor CHD1 binds to SSRP1 both in vivo and in vitro and associates with centromeres. The centromeric localization of CHD1 is lost in SSRP1-depleted cells. RNA interference knockdown of CHD1 leads to a decrease in the amount of centromere localized CENP-A. These findings indicate that the CENP-H–containing complex facilitates deposition of newly synthesized CENP-A into centromeric chromatin in cooperation with FACT and CHD1.

Address correspondence to: Masahiro Okada (maokada{at}tmu.ac.jp).

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