The cenp-t/-w complex is a binding partner of the histone chaperone fact
Prendergast, Lisa ; Müller, Sebastian ; Liu, Yiwei ; Huang, Hongda ; Dingli, Florent ; Loew, Damarys ; Vassias, Isabelle ; Patel, Dinshaw J. ; Sullivan, Kevin F. ; Almouzni, Geneviève
Prendergast, Lisa
Müller, Sebastian
Liu, Yiwei
Huang, Hongda
Dingli, Florent
Loew, Damarys
Vassias, Isabelle
Patel, Dinshaw J.
Sullivan, Kevin F.
Almouzni, Geneviève
Repository DOI
Publication Date
2016-06-01
Type
Article
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Citation
Prendergast, Lisa; Müller, Sebastian; Liu, Yiwei; Huang, Hongda; Dingli, Florent; Loew, Damarys; Vassias, Isabelle; Patel, Dinshaw J. Sullivan, Kevin F.; Almouzni, Geneviève (2016). The cenp-t/-w complex is a binding partner of the histone chaperone fact. Genes & Development 30 (11), 1313-1326
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.
Funder
Publisher
Cold Spring Harbor Laboratory
Publisher DOI
10.1101/gad.275073.115
Rights
Attribution-NonCommercial-NoDerivs 3.0 Ireland