Dynamics of epigenetic control in plants via SET domain containing proteins: Structural and functional insights.
Abiotic stress
Histone
Histone methylation
Plant development
Plant immunity
SET domain
Journal
Biochimica et biophysica acta. Gene regulatory mechanisms
ISSN: 1876-4320
Titre abrégé: Biochim Biophys Acta Gene Regul Mech
Pays: Netherlands
ID NLM: 101731723
Informations de publication
Date de publication:
09 2023
09 2023
Historique:
received:
30
05
2023
revised:
25
07
2023
accepted:
28
07
2023
medline:
18
8
2023
pubmed:
3
8
2023
entrez:
2
8
2023
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 37532097
pii: S1874-9399(23)00061-5
doi: 10.1016/j.bbagrm.2023.194966
pii:
doi:
Substances chimiques
Histones
0
Lysine
K3Z4F929H6
Plant Proteins
0
Chromatin
0
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
194966Informations de copyright
Copyright © 2023 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing interests that could have appeared to influence the work reported in this paper.