| Abstract |
Histone deacetylases are ubiquitous and highly conserved enzymes across all kingdoms of life.
Plant HDAs regulate gene expression and control development and stress response, but little is known about their structure and biochemistry.
Structural and biochemical studies have revealed diverse functions in mammals beyond deacetylation of histones and chromatin remodeling.
A revised and holistic phylogenetic analysis highlights plant HDAs that retain structural characteristics from their bacterial origin and HDAs that have diverged to fulfill potential family-specific functions.
Individual HDAs harbor active-site mutations that have not been identified in mammals or bacteria.
Zn 2+-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.
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