Zn2+-Dependent Histone Deacetylases in Plants: Structure and Evolution

Trends Plant Sci. 2021 Jul;26(7):741-757. doi: 10.1016/j.tplants.2020.12.011. Epub 2021 Jan 15.

Abstract

Zn2+-dependent histone deacetylases are widely distributed in archaea, bacteria, and eukaryotes. Through deacetylation of histones and other biomolecules, these enzymes regulate mammalian gene expression, microtubule stability, and polyamine metabolism. In plants, they play essential roles in development and stress response, but little is known about their biochemistry. We provide here a holistic revision of plant histone deacetylase (HDA) phylogeny and translate recent lessons from other organisms. HDA evolution correlates with a gain of structural ductility/disorder, as observed for other proteins. We also highlight two recently identified Brassicaceae-specific HDAs, as well as unprecedented key mutations that would affect the catalytic activity of individual HDAs. This revised phylogeny will contextualize future studies and illuminate research on plant development and adaptation.

Keywords: ductility; epigenetics; histone deacetylase; intrinsic disorder; plant evolution; zinc-binding.

Publication types

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

MeSH terms

  • Animals
  • Histone Deacetylases* / metabolism
  • Histones
  • Plant Development
  • Plants* / metabolism
  • Zinc

Substances

  • Histones
  • Histone Deacetylases
  • Zinc