Abstract
Nitric oxide (NO) is a key signaling molecule in all kingdoms. In plants, NO is involved in the regulation of various processes of growth and development as well as biotic and abiotic stress response. It mainly acts by modifying protein cysteine or tyrosine residues or by interacting with protein bound transition metals. Thereby, the modification of cysteine residues known as protein S-nitrosation is the predominant mechanism for transduction of NO bioactivity. Histone acetylation on N-terminal lysine residues is a very important epigenetic regulatory mechanism. The transfer of acetyl groups from acetyl-coenzyme A on histone lysine residues is catalyzed by histone acetyltransferases. This modification neutralizes the positive charge of the lysine residue and results in a loose structure of the chromatin accessible for the transcriptional machinery. Histone deacetylases, in contrast, remove the acetyl group of histone tails resulting in condensed chromatin with reduced gene expression activity. In plants, the histone acetylation level is regulated by S-nitrosation. NO inhibits HDA complexes resulting in enhanced histone acetylation and promoting a supportive chromatin state for expression of genes. Moreover, methylation of histone tails and DNA are important epigenetic modifications, too. Interestingly, methyltransferases and demethylases are described as targets for redox molecules in several biological systems suggesting that these types of chromatin modifications are also regulated by NO. In this review article, we will focus on redox-regulation of histone acetylation/methylation and DNA methylation in plants, discuss the consequences on the structural level and give an overview where NO can act to modulate chromatin structure.
Highlights
Methyltransferases and demethylases are described as targets for redox molecules in several biological systems suggesting that these types of chromatin modifications are regulated by Nitric oxide (NO)
We will focus on redox-regulation of histone acetylation/ methylation and DNA methylation in plants, discuss the consequences on the structural level and give an overview where NO can act to modulate chromatin structure
NO synthases (NOS)-like activities have been measured in chloroplasts and peroxisomes of higher plants (He et al, 2004; Corpas and Barroso, 2018), NO synthase has only been identified in the algae (Foresi et al, 2010)
Summary
NO is formed either by reductive or oxidative pathways. In mammals, three cellspecific NO synthases (NOS) oxidize arginine to citrulline, thereby releasing NO. NOS-like activities have been measured in chloroplasts and peroxisomes of higher plants (He et al, 2004; Corpas and Barroso, 2018), NO synthase has only been identified in the algae (Foresi et al, 2010). Nitric Oxide Architects Chromatin Structure to NO constitutes the reductive route of NO production (Rockel et al, 2002; Yamamoto-Katou et al, 2006; Srivastava et al, 2009). Enzyme-independent reduction of nitrite has been described in apoplast under acidic conditions (Bethke et al, 2004). Nuclear NO production is not described in plants. Nuclear translocation of S-nitrosylated proteins is described for gylceralaldehyd-3-phosphat-dehydrogenase and chloride intracellular channel protein CLIC4 (Hara et al, 2005; Malik et al, 2010). Nuclear localization of gylceralaldehyd-3-phosphatdehydrogenase has been characterized in Arabidopsis (Holtgrefe et al, 2008; Vescovi et al, 2013; Aroca et al, 2017)
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