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Nucleic Acids Research 2005 33(9):2868-2879; doi:10.1093/nar/gki579
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Published online 20 May 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
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Article

The CHD remodeling factor Hrp1 stimulates CENP-A loading to centromeres

Julian Walfridsson, Pernilla Bjerling, Maria Thalen, Eung-Jae Yoo1, Sang Dai Park1 and Karl Ekwall*

Karolinska Institute, Department of Biosciences/Department of Natural Sciences, University College Sodertorn Alfred Nobel's Alle 7, S-141 89, Huddinge, Sweden 1School of Biological Sciences, Seoul National University Seoul 151-742, Korea

*To whom correspondence should be addressed. Tel: +46 8 6084713; Fax: +46 8 6084510; Email: karl.ekwall{at}sh.se

Received February 10, 2005. Revised April 27, 2005. Accepted April 27, 2005.

Centromeres of fission yeast are arranged with a central core DNA sequence flanked by repeated sequences. The centromere-associated histone H3 variant Cnp1 (SpCENP-A) binds exclusively to central core DNA, while the heterochromatin proteins and cohesins bind the surrounding outer repeats. CHD (chromo-helicase/ATPase DNA binding) chromatin remodeling factors were recently shown to affect chromatin assembly in vitro. Here, we report that the CHD protein Hrp1 plays a key role at fission yeast centromeres. The hrp1{Delta} mutant disrupts silencing of the outer repeats and central core regions of the centromere and displays chromosome segregation defects characteristic for dysfunction of both regions. Importantly, Hrp1 is required to maintain high levels of Cnp1 and low levels of histone H3 and H4 acetylation at the central core region. Hrp1 interacts directly with the centromere in early S-phase when centromeres are replicated, suggesting that Hrp1 plays a direct role in chromatin assembly during DNA replication.


Present address: Pernilla Bjerling, University of Uppsala, Department IMBIM, Box 582, S-751 23, Uppsala, Sweden


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