Journal
NUCLEIC ACIDS RESEARCH
Volume 42, Issue 10, Pages 6196-6207Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gku263
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Funding
- National Research Foundation of Korea (NRF) - Korea government (MSIP) [2011-0030049]
- National R&D Program for Cancer Control, Ministry for Health, Welfare and Family Affairs, Republic of Korea [0920260]
- Basic Science Research Program through the NRF - Ministry of Education, Science and Technology [2010-0010639]
- NRF - MEST [20090083772]
- Yonsei University Research Fund [2013-12-0087]
- Brain Korea21Plus (BK21+) Program
- Korea Health Promotion Institute [0920260] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- National Research Foundation of Korea [2010-0010639] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Although several studies have suggested that the functions of heterochromatin regulators may be regulated by post-translational modifications during cell cycle progression, regulation of the histone methyltransferase Suv39H1 is not fully understood. Here, we demonstrate a direct link between Suv39H1 phosphorylation and cell cycle progression. We show that CDK2 phosphorylates Suv39H1 at Ser391 and these phosphorylation levels oscillate during the cell cycle, peaking at S phase and maintained during S-G2-M phase. The CDK2-mediated phosphorylation of Suv39H1 at Ser391 results in preferential dissociation from chromatin. Furthermore, phosphorylation-mediated dissociation of Suv39H1 from chromatin causes an enhanced occupancy of JMJD2A histone demethylase on heterochromatin and alterations in inactive histone marks. Overexpression of phospho-mimic Suv39H1 induces early replication of heterochromatin, suggesting the importance of Suv39H1 phosphorylation in the replication of heterochromatin. Moreover, overexpression of phospho-defective Suv39H1 caused altered replication timing of heterochromatin and increases sensitivity to replication stress. Collectively, our data suggest that phosphorylation-mediated modulation of Suv39H1-chromatin association may be an initial step in heterochromatin replication.
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