| Autor: |
Zasadzińska E; Department of Biotechnology and Food Sciences, Lodz University of Technology, Lodz, Poland., Barnhart-Dailey MC, Kuich PH, Foltz DR |
| Jazyk: |
angličtina |
| Zdroj: |
The EMBO journal [EMBO J] 2013 Jul 31; Vol. 32 (15), pp. 2113-24. Date of Electronic Publication: 2013 Jun 14. |
| DOI: |
10.1038/emboj.2013.142 |
| Abstrakt: |
The epigenetic mark of the centromere is thought to be a unique centromeric nucleosome that contains the histone H3 variant, centromere protein-A (CENP-A). The deposition of new centromeric nucleosomes requires the CENP-A-specific chromatin assembly factor HJURP (Holliday junction recognition protein). Crystallographic and biochemical data demonstrate that the Scm3-like domain of HJURP binds a single CENP-A-histone H4 heterodimer. However, several lines of evidence suggest that HJURP forms an octameric CENP-A nucleosome. How an octameric CENP-A nucleosome forms from individual CENP-A/histone H4 heterodimers is unknown. Here, we show that HJURP forms a homodimer through its C-terminal domain that includes the second HJURP_C domain. HJURP exists as a dimer in the soluble preassembly complex and at chromatin when new CENP-A is deposited. Dimerization of HJURP is essential for the deposition of new CENP-A nucleosomes. The recruitment of HJURP to centromeres occurs independent of dimerization and CENP-A binding. These data provide a mechanism whereby the CENP-A pre-nucleosomal complex achieves assembly of the octameric CENP-A nucleosome through the dimerization of the CENP-A chaperone HJURP. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
Plný text