Journal
CELL REPORTS
Volume 11, Issue 1, Pages 22-32Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2015.03.013
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Funding
- la Ligue Nationale contre le Cancer (Equipe Labellisee Ligue)
- European Commission Network of Excellence EpiGeneSys [HEALTH-F4-2010-257082]
- ERC Advanced Grant [2009-AdG_20090506]
- European Commission Large-Scale Integrating [FP7_HEALTH-2010-259743]
- ANR ChromaTin [ANR-10-BLAN-1326-03, ANR-11-LABX-0044_DEEP, ANR-10-IDEX-0001-02 PSL*]
- ANR CHAPINHIB [ANR-12-BSV5-0022-02]
- Aviesan-ITMO Cancer Project Epigenomics of Breast Cancer
- Japan Society for the Promotion of Science
- Marie Curie/Nucleosome 4D
- La Fondation pour la Recherche Medicale
- Agence Nationale de la Recherche (ANR) [ANR-10-BLAN-1326, ANR-11-LABX-0044] Funding Source: Agence Nationale de la Recherche (ANR)
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Although our understanding of centromere maintenance, marked by the histone H3 variant CenH3(CENP-A) in most eukaryotes, has progressed, the mechanism underlying the de novo formation of centromeres remains unclear. We used a synthetic system to dissect how CenH3(CENP-A) contributes to the accumulation of CENP-C and CENP-T, two key components that are necessary for the formation of functional kinetochores. We find that de novo CENP-T accumulation depends on CENP-C and that recruitment of these factors requires two domains in CenH3(CENP-A): the HJURP-binding region (CATD) and the CENP-C-binding region (CAC). Notably, HJURP interacts directly with CENP-C and is critical for de novo accumulation of CENP-C at synthetic centromeres. On the basis of our findings, we propose that HJURP serves a dual chaperone function in coordinating CenH3(CENP-A) and CENP-C recruitment.
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