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Published online March 5, 2007
doi:10.1083/jcb.200701065
The Journal of Cell Biology, Vol. 176, No. 6, 757-763
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Maddox et al.
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 Functional genomics identifies a Myb domain–containing protein family required for assembly of CENP-A chromatin

Paul S. Maddox, Francie Hyndman, Joost Monen, Karen Oegema, and Arshad Desai

Ludwig Institute for Cancer Research, Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093

Correspondence to Arshad Desai: abdesai{at}ucsd.edu; or Paul S. Maddox: pmaddox{at}ucsd.edu

Nucleosomes containing the centromere-specific histone H3 variant centromere protein A (CENP-A) create the chromatin foundation for kinetochore assembly. To understand the mechanisms that selectively target CENP-A to centromeres, we took a functional genomics approach in the nematode Caenorhabditis elegans, in which failure to load CENP-A results in a signature kinetochore-null (KNL) phenotype. We identified a single protein, KNL-2, that is specifically required for CENP-A incorporation into chromatin. KNL-2 and CENP-A localize to centromeres throughout the cell cycle in an interdependent manner and coordinately direct chromosome condensation, kinetochore assembly, and chromosome segregation. The isolation of KNL-2–associated chromatin coenriched CENP-A, indicating their close proximity on DNA. KNL-2 defines a new conserved family of Myb DNA-binding domain–containing proteins. The human homologue of KNL-2 is also specifically required for CENP-A loading and kinetochore assembly but is only transiently present at centromeres after mitotic exit. These results implicate a new protein class in the assembly of centromeric chromatin and suggest that holocentric and monocentric chromosomes share a common mechanism for CENP-A loading.

Abbreviations used in this paper: CENP-A, centromere protein A; DIC, differential interference contrast; dsRNA, double-stranded RNA; KNL, kinetochore null.


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