Dynamics of epigenetic control in plants via SET domain containing proteins: Structural and functional insights

Biochim Biophys Acta Gene Regul Mech. 2023 Sep;1866(3):194966. doi: 10.1016/j.bbagrm.2023.194966. Epub 2023 Jul 31.

Abstract

Plants control expression of their genes in a way that involves manipulating the chromatin structural dynamics in order to adapt to environmental changes and carry out developmental processes. Histone modifications like histone methylation are significant epigenetic marks which profoundly and globally modify chromatin, potentially affecting the expression of several genes. Methylation of histones is catalyzed by histone lysine methyltransferases (HKMTs), that features an evolutionary conserved domain known as SET [Su(var)3-9, E(Z), Trithorax]. This methylation is directed at particular lysine (K) residues on H3 or H4 histone. Plant SET domain group (SDG) proteins are categorized into different classes that have been conserved through evolution, and each class have specificity that influences how the chromatin structure operates. The domains discovered in plant SET domain proteins have typically been linked to protein-protein interactions, suggesting that majority of the SDGs function in complexes. Additionally, SDG-mediated histone mark deposition also affects alternative splicing events. In present review, we discussed the diversity of SDGs in plants including their structural properties. Additionally, we have provided comprehensive summary of the functions of the SDG-domain containing proteins in plant developmental processes and response to environmental stimuli have also been highlighted.

Keywords: Abiotic stress; Histone; Histone methylation; Plant development; Plant immunity; SET domain.

Publication types

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

MeSH terms

  • Chromatin / genetics
  • Epigenesis, Genetic
  • Histones* / metabolism
  • Lysine* / metabolism
  • PR-SET Domains
  • Plant Proteins / metabolism
  • Plants / genetics

Substances

  • Histones
  • Lysine
  • Plant Proteins
  • Chromatin