The CENP-T/-W complex is a binding partner of the histone chaperone FACT Journal Article
| Authors: | Prendergast, L.; Müller, S.; Liu, Y.; Huang, H.; Dingli, F.; Loew, D.; Vassias, I.; Patel, D. J.; Sullivan, K. F.; Almouzni, G. |
| Article Title: | The CENP-T/-W complex is a binding partner of the histone chaperone FACT |
| Abstract: | The CENP-T/-W histone fold complex, as an integral part of the inner kinetochore, is essential for building a proper kinetochore at the centromere in order to direct chromosome segregation during mitosis. Notably, CENP-T/-W is not inherited at centromeres, and new deposition is absolutely required at each cell cycle for kinetochore function. However, the mechanisms underlying this new deposition of CENP-T/-W at centromeres are unclear. Here, we found that CENP-T deposition at centromeres is uncoupled from DNA synthesis. We identified Spt16 and SSRP1, subunits of the H2A–H2B histone chaperone facilitates chromatin transcription (FACT), as CENP-W binding partners through a proteomic screen. We found that the C-terminal region of Spt16 binds specifically to the histone fold region of CENP-T/-W. Furthermore, depletion of Spt16 impairs CENP-T and CENP-W deposition at endogenous centromeres, and site-directed targeting of Spt16 alone is sufficient to ensure local de novo CENP-T accumulation. We propose a model in which the FACT chaperone stabilizes the soluble CENP-T/-W complex in the cell and promotes dynamics of exchange, enabling CENP-T/-W deposition at centromeres. © 2016 Nemajerova et al. |
| Keywords: | mitosis; centromere; histone chaperone; cenp |
| Journal Title: | Genes and Development |
| Volume: | 30 |
| Issue: | 11 |
| ISSN: | 0890-9369 |
| Publisher: | Cold Spring Harbor Laboratory Press |
| Date Published: | 2016-06-01 |
| Start Page: | 1313 |
| End Page: | 1326 |
| Language: | English |
| DOI: | 10.1101/gad.275073.115 |
| PROVIDER: | scopus |
| PMCID: | PMC4911930 |
| PUBMED: | 27284163 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 1 July 2016 -- Source: Scopus |
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