期刊
NUCLEIC ACIDS RESEARCH
卷 43, 期 19, 页码 9097-9106出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkv929
关键词
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资金
- Comision Nacional de Ciencia y Tecnologia [FONDECYT 1120170, PFB16, ACT1119]
- PCHA/Doctorado Nacional [2014-21140324, 2014-21140346]
- Chineses Scholarship Council (CSC)
- DFG [CRC1064-Z2]
- La Ligue Nationale contre le Cancer [Equipe labellisee Ligue and a postdoctoral fellowship]
- European Commission Network of Excellence Epi-GeneSys [HEALTH-F4-2010-257082]
- ERC [2009-AdG_20090506]
- European Commission large-scale integrating project [FP7_HEALTH-2010-259743]
- ANR 'ChromaTin' [ANR-10-BLAN-1326-03, ANR-11-LABX-0044_DEEP, ANR-10-IDEX-0001-02 PSL*]
- ANR 'CHAPINHIB' [ANR-12-BSV5-0022-02]
- Aviesan-ITMO Cancer Project 'Epigenomics of breast cancer'
- Agence Nationale de la Recherche (ANR) [ANR-11-LABX-0044, ANR-10-BLAN-1326] Funding Source: Agence Nationale de la Recherche (ANR)
Histone post-translational modifications are key contributors to chromatin structure and function, and participate in the maintenance of genome stability. Understanding the establishment and maintenance of these marks, along with their misregulation in pathologies is thus a major focus in the field. While we have learned a great deal about the enzymes regulating histone modifications on nucleosomal histones, much less is known about the mechanisms establishing modifications on soluble newly synthesized histones. This includes methylation of lysine 9 on histone H3 (H3K9), a mark that primes the formation of heterochromatin, a critical chromatin landmark for genome stability. Here, we report that H3K9 mono- and dimethylation is imposed during translation by the methyltransferase SetDB1. We discuss the importance of these results in the context of heterochromatin establishment and maintenance and new therapeutic opportunities in pathologies where heterochromatin is perturbed.
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