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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.
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Submitted on : Wednesday, June 15, 2016 - 2:29:09 PM
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Lisa Prendergast, Sebastian Müller, Yiwei Liu, Hongda Huang, Florent Dingli, et al.. The CENP-T/-W complex is a binding partner of the histone chaperone FACT. Genes and Development, Cold Spring Harbor Laboratory Press, 2016, 30 (11), pp.1313-1326 ⟨10.1101/gad.275073.115⟩. ⟨hal-01332229⟩



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