CENP-C and CENP-I are key connecting factors for kinetochore and CENP-A assembly

Although it is generally accepted that chromatin containing the histone H3 variant CENP-A is an epigenetic mark maintaining centromere identity, the pathways leading to the formation and maintenance of centromere chromatin remain unclear. We previously generated human artificial chromosomes (HACs) w...

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Veröffentlicht in:Journal of cell science 2015-12, Vol.128 (24), p.4572-4587
Hauptverfasser: Shono, Nobuaki, Ohzeki, Jun-ichirou, Otake, Koichiro, Martins, Nuno M C, Nagase, Takahiro, Kimura, Hiroshi, Larionov, Vladimir, Earnshaw, William C, Masumoto, Hiroshi
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container_end_page 4587
container_issue 24
container_start_page 4572
container_title Journal of cell science
container_volume 128
creator Shono, Nobuaki
Ohzeki, Jun-ichirou
Otake, Koichiro
Martins, Nuno M C
Nagase, Takahiro
Kimura, Hiroshi
Larionov, Vladimir
Earnshaw, William C
Masumoto, Hiroshi
description Although it is generally accepted that chromatin containing the histone H3 variant CENP-A is an epigenetic mark maintaining centromere identity, the pathways leading to the formation and maintenance of centromere chromatin remain unclear. We previously generated human artificial chromosomes (HACs) whose centromeres contain a synthetic alpha-satellite (alphoid) DNA array containing the tetracycline operator (alphoid(tetO)). We also obtained cell lines bearing the alphoid(tetO) array at ectopic integration sites on chromosomal arms. Here, we have examined the regulation of CENP-A assembly at centromeres as well as de novo assembly on the ectopic arrays by tethering tetracycline repressor (tetR) fusions of substantial centromeric factors and chromatin modifiers. This analysis revealed four classes of factors that influence CENP-A assembly. Interestingly, many kinetochore structural components induced de novo CENP-A assembly at the ectopic site. We showed that these components work by recruiting CENP-C and subsequently recruiting M18BP1. Furthermore, we found that CENP-I can also recruit M18BP1 and, as a consequence, enhances M18BP1 assembly on centromeres in the downstream of CENP-C. Thus, we suggest that CENP-C and CENP-I are key factors connecting kinetochore to CENP-A assembly.
doi_str_mv 10.1242/jcs.180786
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subjects Autoantigens - genetics
Autoantigens - metabolism
Centromere Protein A
Chromosomal Proteins, Non-Histone - genetics
Chromosomal Proteins, Non-Histone - metabolism
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
HeLa Cells
Humans
Kinetochores - metabolism
title CENP-C and CENP-I are key connecting factors for kinetochore and CENP-A assembly
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