HJURP is a CENP-A chromatin assembly factor sufficient to form a functional de novo kinetochore

Meghan C. Barnhart, P. Henning J L Kuich, Madison E. Stellfox, Jared A. Ward, Emily A. Bassett, Ben E. Black, Daniel R. Foltz*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

206 Scopus citations

Abstract

Centromeres of higher eukaryotes are epigenetically marked by the centromere-specific CENP-A nucleosome. New CENP-A recruitment requires the CENP-A histone chaperone HJURP. In this paper, we show that a LacI (Lac repressor) fusion of HJURP drove the stable recruitment of CENP-A to a LacO (Lac operon) array at a noncentromeric locus. Ectopically targeted CENP-A chromatin at the LacO array was sufficient to direct the assembly of a functional centromere as indicated by the recruitment of the constitutive centromereassociated network proteins, the microtubule-binding protein NDC80, and the formation of stable kinetochore-microtubule attachments. An amino-terminal fragment of HJURP was able to assemble CENP-A nucleosomes in vitro, demonstrating that HJURP is a chromatin assembly factor. Furthermore, HJURP recruitment to endogenous centromeres required the Mis18 complex. Together, these data suggest that the role of the Mis18 complex in CENP-A deposition is to recruit HJURP and that the CENP-A nucleosome assembly activity of HJURP is responsible for centromeric chromatin assembly to maintain the epigenetic mark.

Original languageEnglish (US)
Pages (from-to)229-243
Number of pages15
JournalJournal of Cell Biology
Volume194
Issue number2
DOIs
StatePublished - Jul 25 2011

ASJC Scopus subject areas

  • Cell Biology

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