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The CENP-T/-W complex is a binding partner of the histone chaperone FACT
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 a...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4911930/ https://www.ncbi.nlm.nih.gov/pubmed/27284163 http://dx.doi.org/10.1101/gad.275073.115 |
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author | Prendergast, Lisa Müller, Sebastian Liu, Yiwei Huang, Hongda Dingli, Florent Loew, Damarys Vassias, Isabelle Patel, Dinshaw J. Sullivan, Kevin F. Almouzni, Geneviève |
author_facet | Prendergast, Lisa Müller, Sebastian Liu, Yiwei Huang, Hongda Dingli, Florent Loew, Damarys Vassias, Isabelle Patel, Dinshaw J. Sullivan, Kevin F. Almouzni, Geneviève |
author_sort | Prendergast, Lisa |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4911930 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-49119302016-07-06 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 Genes Dev Research Paper 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. Cold Spring Harbor Laboratory Press 2016-06-01 /pmc/articles/PMC4911930/ /pubmed/27284163 http://dx.doi.org/10.1101/gad.275073.115 Text en © 2016 Prendergast et al.; Published by Cold Spring Harbor Laboratory Press http://creativecommons.org/licenses/by/4.0/ This article, published in Genes & Development, is available under a Creative Commons License (Attribution 4.0 International), as described at http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Research Paper Prendergast, Lisa Müller, Sebastian Liu, Yiwei Huang, Hongda Dingli, Florent Loew, Damarys Vassias, Isabelle Patel, Dinshaw J. Sullivan, Kevin F. Almouzni, Geneviève The CENP-T/-W complex is a binding partner of the histone chaperone FACT |
title | The CENP-T/-W complex is a binding partner of the histone chaperone FACT |
title_full | The CENP-T/-W complex is a binding partner of the histone chaperone FACT |
title_fullStr | The CENP-T/-W complex is a binding partner of the histone chaperone FACT |
title_full_unstemmed | The CENP-T/-W complex is a binding partner of the histone chaperone FACT |
title_short | The CENP-T/-W complex is a binding partner of the histone chaperone FACT |
title_sort | cenp-t/-w complex is a binding partner of the histone chaperone fact |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4911930/ https://www.ncbi.nlm.nih.gov/pubmed/27284163 http://dx.doi.org/10.1101/gad.275073.115 |
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