CENP-T-W-S-X Forms a Unique Centromeric Chromatin Structure with a Histone-like Fold
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Cheeseman_CENP-T-W-S-X.pdf
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Author(s)
Nishino, Tatsuya
Takeuchi, Kozo
Gascoigne, Karen E.
Suzuki, Aussie
Hori, Tetsuya
Oyama, Takuji
Morikawa, Kosuke
Fukagawa, Tatsuo
Cheeseman, Iain M
Date Issued
February 2012
Journal
Cell
Publisher
Elsevier
Citation
Nishino, Tatsuya, Kozo Takeuchi, Karen E. Gascoigne, Aussie Suzuki, Tetsuya Hori, Takuji Oyama, Kosuke Morikawa, Iain M. Cheeseman, and Tatsuo Fukagawa. “CENP-T-W-S-X Forms a Unique Centromeric Chromatin Structure with a Histone-like Fold.” Cell 148, no. 3 (February 2012): 487-501. Copyright © 2012 Elsevier Inc.
Version
Final published version
Abstract
The multiprotein kinetochore complex must assemble at a specific site on each chromosome to achieve accurate chromosome segregation. Defining the nature of the DNA-protein interactions that specify the position of the kinetochore and provide a scaffold for kinetochore formation remain key goals. Here, we demonstrate that the centromeric histone-fold-containing CENP-T-W and CENP-S-X complexes coassemble to form a stable CENP-T-W-S-X heterotetramer. High-resolution structural analysis of the individual complexes and the heterotetramer reveals similarity to other histone fold-containing complexes including canonical histones within a nucleosome. The CENP-T-W-S-X heterotetramer binds to and supercoils DNA. Mutants designed to compromise heterotetramerization or the DNA-protein contacts around the heterotetramer strongly reduce the DNA binding and supercoiling activities in vitro and compromise kinetochore assembly in vivo. These data suggest 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.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Whitehead Institute for Biomedical Research
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DOI of Published Version
https://doi.org/10.1016/j.cell.2011.11.061
