HJURP Involvement in De Novo CenH3CENP-A and CENP-C Recruitment
| Autor: | Kerstin Klare, Hiroaki Tachiwana, Geneviève Almouzni, Julia Blümer, Andrea Musacchio, Sebastian Müller |
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| Přispěvatelé: | Université Paris sciences et lettres (PSL), Dynamique du noyau, Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Max Planck Institute of Molecular Physiology, Max-Planck-Gesellschaft, HAL-UPMC, Gestionnaire |
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Chromosomal Proteins
Non-Histone Centromere macromolecular substances [SDV.BC]Life Sciences [q-bio]/Cellular Biology Autoantigens General Biochemistry Genetics and Molecular Biology Histones 03 medical and health sciences Histone H3 0302 clinical medicine Centromere Protein A Humans Kinetochores [SDV.BC] Life Sciences [q-bio]/Cellular Biology lcsh:QH301-705.5 030304 developmental biology Genetics 0303 health sciences biology Kinetochore Nucleosomes Cell biology DNA-Binding Proteins lcsh:Biology (General) Chaperone (protein) biology.protein Biologie 030217 neurology & neurosurgery Molecular Chaperones Protein Binding |
| Zdroj: | Cell Reports Cell Reports, 2015, 11 (1), pp.22-32. ⟨10.1016/j.celrep.2015.03.013⟩ Cell Reports, Elsevier Inc, 2015, 11 (1), pp.22-32. ⟨10.1016/j.celrep.2015.03.013⟩ Cell Reports, Vol 11, Iss 1, Pp 22-32 (2015) |
| ISSN: | 2211-1247 |
| DOI: | 10.1016/j.celrep.2015.03.013⟩ |
| Popis: | International audience; Although our understanding of centromere maintenance, marked by the histone H3 variant CenH3CENP-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 CenH3CENP-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 CenH3CENP-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 CenH3CENP-A and CENP-C recruitment. |
| Databáze: | OpenAIRE |
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