| Autor: |
Barnhart MC; Department of Biochemistry and Molecular Genetics, University of Virginia Medical School, Charlottesville, VA 22908, USA., Kuich PH, Stellfox ME, Ward JA, Bassett EA, Black BE, Foltz DR |
| Jazyk: |
angličtina |
| Zdroj: |
The Journal of cell biology [J Cell Biol] 2011 Jul 25; Vol. 194 (2), pp. 229-43. Date of Electronic Publication: 2011 Jul 18. |
| DOI: |
10.1083/jcb.201012017 |
| Abstrakt: |
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 centromere-associated 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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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