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CENP-T-W-S-X forms a unique centromeric chromatin structure with a histone-like folds

 Press Release 

Cell

Department of Molecular Genetics, National Institute of Genetics
CENP-T-W-S-X forms a unique centromeric chromatin structure with a histone-like folds
Tatsuya Nishino, Kozo Takeuchi, Karen E. Gascoigne, Aussie Suzuki, Tetsuya Hori, Takuji Oyama, Kosuke Morikawa, Iain M. Cheeseman, and Tatsuo Fukagawa,
Cell, Feb 3rd issue  DOI: 10.1016/j.cell.2011.11.061

Accurate chromosome segregation during mitosis requires the assembly of a multi-protein kinetochore complex to contact centromeric DNA. We demonstrate that the centromeric histone-fold containing CENP-T-W and CENP-S-X complexes co-assemble to form a stable CENP-T-W-S-X heterotetramer at kinetochores. As the heterotetramer has a number of structural and functional similarities with canonical histones, we propose that the CENP-T-W-S-X complex forms a unique nucleosome-like structure to generate contacts with DNA, extending the “histone code” beyond canonical nucleosome proteins.
  

A (CENP-S-X)2 tetramer interacts with a CENP-T-W dimer and CENP-S-X alternately co-assembles with the CENP-T-W dimer to form a stable CENP-T-W-S-X heterotetramer.  The CENP-T-W-S-X complex binds to ~100bp nucleosome free DNA and forms a nucleosome-like structure, which functions as a structural scaffold for kinetochore assembly.