Structure and function of histone methylation-binding proteins in plants

Biochem J. 2016 Jun 15;473(12):1663-80. doi: 10.1042/BCJ20160123.

Abstract

Post-translational modifications of histones play important roles in modulating many essential biological processes in both animals and plants. These covalent modifications, including methylation, acetylation, phosphorylation, ubiquitination, SUMOylation and so on, are laid out and erased by histone-modifying enzymes and read out by effector proteins. Recent studies have revealed that a number of developmental processes in plants are under the control of histone post-translational modifications, such as floral transition, seed germination, organogenesis and morphogenesis. Therefore, it is critical to identify those protein domains, which could specifically recognize these post-translational modifications to modulate chromatin structure and regulate gene expression. In the present review, we discuss the recent progress in understanding the structure and function of the histone methylation readers in plants, by focusing on Arabidopsis thaliana proteins.

Keywords: epigenetics; histone methylation readers; histone post-translational modifications.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis Proteins / chemistry
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism
  • Histones / metabolism*
  • Methylation
  • Plant Proteins / chemistry
  • Plant Proteins / genetics
  • Plant Proteins / metabolism*
  • Plants / metabolism*
  • Protein Processing, Post-Translational

Substances

  • Arabidopsis Proteins
  • Histones
  • Plant Proteins