Journal
SCIENCE
Volume 343, Issue 6176, Pages 1249-1253Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1248357
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Funding
- Louis-Berlinguet postdoctoral fellowship (Fonds Quebecois de la Recherche en Sante/Genome Quebec)
- Deutsche Akademie der Naturforscher Leopoldina [LPDS 2009-5]
- Empire State Training Program in Stem Cell Research (NYSTEM) [C026880]
- NIH [GM064844, R37GM037120, GM075060, GM067014]
- Howard Hughes Medical Institute
- Natural Sciences and Engineering Research Council of Canada [191666]
- Howard Hughes Medical Institute-Gordon
- Betty Moore Foundation
- NSF [DBI-1025830]
- Direct For Biological Sciences
- Division Of Integrative Organismal Systems [1025830] Funding Source: National Science Foundation
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Histone variants have been proposed to act as determinants for posttranslational modifications with widespread regulatory functions. We identify a histone-modifying enzyme that selectively methylates the replication-dependent histone H3 variant H3.1. The crystal structure of the SET domain of the histone H3 lysine-27 (H3K27) methyltransferase ARABIDOPSIS TRITHORAX-RELATED PROTEIN 5 (ATXR5) in complex with a H3.1 peptide shows that ATXR5 contains a bipartite catalytic domain that specifically reads alanine-31 of H3.1. Variation at position 31 between H3.1 and replication-independent H3.3 is conserved in plants and animals, and threonine-31 in H3.3 is responsible for inhibiting the activity of ATXR5 and its paralog, ATXR6. Our results suggest a simple model for the mitotic inheritance of the heterochromatic mark H3K27me1 and the protection of H3.3-enriched genes against heterochromatization during DNA replication.
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