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Redox-dependent chromatin remodeling: A new function of nitric oxide as architect of chromatin structure in plants.

Front. Plant Sci. 10:625 (2019)
Verlagsversion DOI
Open Access Gold
Creative Commons Lizenzvertrag
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.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Schlagwörter S-nitrosation ; Acetylation ; Chromatin Modulation ; Methylation ; Nitric Oxide ; Redox-modification; L-homocysteine Hydrolase; S-nitrosylated Proteins; Cytosolic Glyceraldehyde-3-phosphate Dehydrogenase; Dna Methylation; Gene-expression; Cell-death; Nuclear Translocation; Histone Deacetylases; Arabidopsis-thaliana; Transcription Factor
ISSN (print) / ISBN 1664-462X
e-ISSN 1664-462X
Quellenangaben Band: 10, Heft: , Seiten: , Artikelnummer: 625 Supplement: ,
Verlag Frontiers
Verlagsort Avenue Du Tribunal Federal 34, Lausanne, Ch-1015, Switzerland
Begutachtungsstatus Peer reviewed