西亚试剂：Selective Methylation of Histone H3 Variant H3.1 Regulates

Selective Methylation of Histone H3 Variant H3.1 Regulates Heterochromatin Replication

Yannick Jacob1，*， Elisa Bergamin2，*， Mark T. A. Donoghue1， Vanessa Mongeon2， Chantal LeBlanc1， Philipp Voigt3， Charles J. Underwood1， Joseph S. Brunzelle4， Scott D. Michaels5， Danny Reinberg3， Jean-Fran？ois Couture2，？， Robert A. Martienssen1，6，？

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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