Abstract
Plants tightly control gene transcription to adapt to environmental conditions and steer growth and development. Different types of epigenetic modifications are instrumental in these processes. In recent years, an important role for the chromatin-modifying RPD3/HDA1 class I HDAC HISTONE DEACETYLASE 9 (HDA9) emerged in the regulation of a multitude of plant traits and responses. HDACs are widely considered transcriptional repressors and are typically part of multiprotein complexes containing co-repressors, DNA, and histone-binding proteins. By catalyzing the removal of acetyl groups from lysine residues of histone protein tails, HDA9 negatively controls gene expression in many cases, in concert with interacting proteins such as POWERDRESS (PWR), HIGH EXPRESSION OF OSMOTICALLY RESPONSIVE GENES 15 (HOS15), WRKY53, ELONGATED HYPOCOTYL 5 (HY5), ABA INSENSITIVE 4 (ABI4), and EARLY FLOWERING 3 (ELF3). However, HDA9 activity has also been directly linked to transcriptional activation. In addition, following the recent breakthrough discovery of mutual negative feedback regulation between HDA9 and its interacting WRKY-domain transcription factor WRKY53, swift progress in gaining understanding of the biology of HDA9 is expected. In this review, we summarize knowledge on this intriguing versatile-and long under-rated-protein and propose novel leads to further unravel HDA9-governed molecular networks underlying plant development and environmental biology.
Highlights
Eukaryotic DNA is orderly and densely packed into higher order structures, called chromatin
In Arabidopsis thaliana, there are 18 proteins recognized as histone deacetylases (HDACs) that are categorized into three families: the Reduced Potassium Dependence3 (RPD3/HDA1-like) family, the plant-specific HD2type family,and the NAD-dependent Silent Information Regulator (SIR) family
We report in detail the intriguing findings on the versatile role of the pleiotropic HISTONE DEACETYLASE 9 (HDA9) chromatinmodifying protein (Fig. 1) and discuss possible future directions required to further unravel the function and regulation of HDA9-governed molecular networks
Summary
Peter G.H. de Rooij1,†, Giorgio Perrella2,3,†, Eirini Kaiserli, and Martijn van Zanten1,*, 1 Molecular Plant Physiology, Institute of Environmental Biology, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands 2 Institute of Molecular, Cell & Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK 3 ENEA - Trisaia Research Centre 75026, Rotondella (Matera), Italy
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