Selective methylation of histone H3 variant H3.1 regulates heterochromatin replication

Yannick Jacob, Elisa Bergamin, Mark T A Donoghue, Vanessa Mongeon, Chantal LeBlanc, Philipp Voigt, Charles J Underwood, Joseph S Brunzelle, Scott D Michaels, Danny Reinberg, Jean-François Couture, Robert A Martienssen

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)1249-1253
Number of pages5
JournalScience
Volume343
Issue number6176
DOIs
Publication statusPublished - 14 Mar 2014

Keywords

  • amino acid sequence
  • arabidopsis
  • arabidopsis proteins
  • catalytic domain
  • conserved sequence
  • crystallography
  • DNA replication
  • epigenesis
  • gene expression regulation
  • heterochromatin
  • histones
  • methylation
  • methyltransferases
  • mitosis
  • molecular sequence data
  • protein processing
  • threonine
  • post-translational
  • x-Ray

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