Peer-Reviewed Journal Details
Mandatory Fields
Prendergast, L,Muller, S,Liu, YW,Huang, HD,Dingli, F,Loew, D,Vassias, I,Patel, DJ,Sullivan, KF,Almouzni, G
2016
June
Genes & Development
The CENP-T/-W complex is a binding partner of the histone chaperone FACT
Published
Altmetric: 7WOS: 15 ()
Optional Fields
centromere CENP histone chaperone mitosis HUMAN-CELLS CENTROMERIC CHROMATIN A NUCLEOSOMES SACCHAROMYCES-CEREVISIAE OUTER KINETOCHORE STRUCTURAL BASIS TRANSCRIPTION RECRUITMENT RNA MAINTENANCE
30
1313
1326
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.
10.1101/gad.275073.115
Grant Details
Publication Themes