Journal
DEVELOPMENTAL CELL
Volume 37, Issue 5, Pages 413-427Publisher
CELL PRESS
DOI: 10.1016/j.devcel.2016.05.006
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Funding
- MEXT KAKENHI grants [23247030, 23114008, 16H04747, 16H01414]
- Kazusa DNA Research Institute Foundation
- Wellcome Trust [073915]
- Japan Society for the Promotion of Science
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- NIH, National Cancer Institute
- Center for Cancer Research
- Grants-in-Aid for Scientific Research [16H01414, 23247030, 16H04747] Funding Source: KAKEN
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Centromere chromatin containing histone H3 variant CENP-A is required for accurate chromosome segregation as a foundation for kinetochore assembly. Human centromere chromatin assembles on a part of the long a-satellite (alphoid) DNA array, where it is flanked by pericentric heterochromatin. Heterochromatin spreads into adjacent chromatin and represses gene expression, and it can antagonize centromere function or CENP-A assembly. Here, we demonstrate an interaction between CENP-A assembly factor M18BP1 and acetyltransferase KAT7/HBO1/MYST2. Knocking out KAT7 in HeLa cells reduced centromeric CENP-A assembly. Mitotic chromosome misalignment and micronuclei formation increased in the knockout cells and were enhanced when the histone H3-K9 trimethylase Suv39h1 was overproduced. Tethering KAT7 to an ectopic alphoid DNA integration site removed heterochromatic H3K9me3 modification and was sufficient to stimulate new CENP-A or histone H3.3 assembly. Thus, KAT7-containing acetyltransferases associating with the Mis18 complex provides competence for histone turnover/exchange activity on alphoid DNA and prevents Suv39h1-mediated heterochromatin invasion into centromeres.
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