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Published online December 1, 2008
doi:10.1083/jcb.200806038
The Journal of Cell Biology, Vol. 183, No. 5, 805-818
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Erhardt et al.
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Article

Genome-wide analysis reveals a cell cycle–dependent mechanism controlling centromere propagation



Sylvia Erhardt1,2,4, Barbara G. Mellone1,2, Craig M. Betts3, Weiguo Zhang1,2, Gary H. Karpen1,2, and Aaron F. Straight3

1 Department of Genome Dynamics, Lawrence Berkeley National Laboratory and 2 Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720
3 Department of Biochemistry, Stanford Medical School, Stanford, CA 94305
4 Zentrum für Molekulare Biologie, Universität Heidelberg, D-69120 Heidelberg, Germany

Correspondence to Aaron F. Straight: astraigh{at}stanford.edu

Centromeres are the structural and functional foundation for kinetochore formation, spindle attachment, and chromosome segregation. In this study, we isolated factors required for centromere propagation using genome-wide RNA interference screening for defects in centromere protein A (CENP-A; centromere identifier [CID]) localization in Drosophila melanogaster. We identified the proteins CAL1 and CENP-C as essential factors for CID assembly at the centromere. CID, CAL1, and CENP-C coimmunoprecipitate and are mutually dependent for centromere localization and function. We also identified the mitotic cyclin A (CYCA) and the anaphase-promoting complex (APC) inhibitor RCA1/Emi1 as regulators of centromere propagation. We show that CYCA is centromere localized and that CYCA and RCA1/Emi1 couple centromere assembly to the cell cycle through regulation of the fizzy-related/CDH1 subunit of the APC. Our findings identify essential components of the epigenetic machinery that ensures proper specification and propagation of the centromere and suggest a mechanism for coordinating centromere inheritance with cell division.

S. Erhardt, B.G. Mellone, and C.M. Betts contributed equally to this paper.

B.G. Mellone's present address is Dept. of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269.

Abbreviations used in this paper: APC, anaphase-promoting complex; β-ME, β-mercaptoethanol; BTP, bromothenylpteridine; CENP, centromere protein; CID, centromere identifier; CLD, CID localization deficient; CYCA, cyclin A; DOTAP, 1,2-dioleoyl-3-trimethylammonium-propane; dsRNA, double-stranded RNA; FZR, FZY related; FZY, fizzy; IF, immunofluorescence; LAP, localization and purification; LPC, leupeptin, pepstatin, and chymostatin; Rod, rough deal; TMR*, tetramethyl rhodamine*.

© 2008 Erhardt et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).


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