CENP-B creates alternative epigenetic chromatin states permissive for CENP-A or heterochromatin assembly
| Autor: | Otake, K., Ohzeki, J. I., Shono, N., Kugou, K., Okazaki, K., Nagase, T., Yamakawa, H., Kouprina, N., Larionov, V., Kimura, Hiroshi, Earnshaw, W. C., Masumoto, H. |
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| Rok vydání: | 2020 |
| Předmět: |
ASH1L
Alternative epigenetic states Chromosomal Proteins Non-Histone Satellite DNA Heterochromatin Centromere macromolecular substances Biology Autoantigens Hp1 Epigenesis Genetic 03 medical and health sciences 0302 clinical medicine Humans Nucleosome Heterochromatin assembly Ash1l 030304 developmental biology ASH1l 0303 health sciences HP1 alternative epigenetic states Acidic-rich domain Cell Biology Chromatin Cell biology Histone centromere Chromobox Protein Homolog 5 Cenp-b biology.protein Heterochromatin protein 1 Centromere Protein A CENP-B 030217 neurology & neurosurgery acidic rich domain Research Article |
| Zdroj: | Journal of Cell Science article-version (VoR) Version of Record Otake, K, Ohzeki, J, Shono, N, Kugou, K, Okazaki, K, Nagase, T, Yamakawa, H, Kouprina, N, Larionov, V, Kimura, H, Earnshaw, W C & Masumoto, H 2020, ' CENP-B creates alternative epigenetic chromatin states permissive for CENP-A or heterochromatin assembly ', Journal of Cell Science, vol. 133, jcs.243303 . https://doi.org/10.1242/jcs.243303 |
| ISSN: | 1477-9137 0021-9533 |
| Popis: | CENP-B binds to CENP-B boxes on centromeric satellite DNAs (known as alphoid DNA in humans). CENP-B maintains kinetochore function through interactions with CENP-A nucleosomes and CENP-C. CENP-B binding to transfected alphoid DNA can induce de novo CENP-A assembly, functional centromere and kinetochore formation, and subsequent human artificial chromosome (HAC) formation. Furthermore, CENP-B also facilitates H3K9 (histone H3 lysine 9) trimethylation on alphoid DNA, mediated by Suv39h1, at ectopic alphoid DNA integration sites. Excessive heterochromatin invasion into centromere chromatin suppresses CENP-A assembly. It is unclear how CENP-B controls such different chromatin states. Here, we show that the CENP-B acidic domain recruits histone chaperones and many chromatin modifiers, including the H3K36 methylase ASH1L, as well as the heterochromatin components Suv39h1 and HP1 (HP1α, β and γ, also known as CBX5, CBX1 and CBX3, respectively). ASH1L facilitates the formation of open chromatin competent for CENP-A assembly on alphoid DNA. These results indicate that CENP-B is a nexus for histone modifiers that alternatively promote or suppress CENP-A assembly by mutually exclusive mechanisms. Besides the DNA-binding domain, the CENP-B acidic domain also facilitates CENP-A assembly de novo on transfected alphoid DNA. CENP-B therefore balances CENP-A assembly and heterochromatin formation on satellite DNA. Summary: The acidic domain of CENP-B facilitates assembly of various proteins at centromeric satellite DNA, including HP1 and ASH1L. CENP-B controls centromere epigenetic status. |
| Databáze: | OpenAIRE |
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