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Rudolf, E.E. ; Hüther, P.* ; Forne, I.* ; Georgii, E. ; Han, Y. ; Hell, R.* ; Wirtz, M.* ; Imhof, A.* ; Becker, C.* ; Durner, J. ; Lindermayr, C.

Gsnor contributes to demethylation and expression of transposable elements and stress-responsive genes.

Antioxidants 10:1128 (2021)

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In the past, reactive nitrogen species (RNS) were supposed to be stress-induced by-products of disturbed metabolism that cause oxidative damage to biomolecules. However, emerging evidence demonstrates a substantial role of RNS as endogenous signals in eukaryotes. In plants, S-nitrosoglutathione (GSNO) is the dominant RNS and serves as the •NO donor for S-nitrosation of diverse effector proteins. Remarkably, the endogenous GSNO level is tightly controlled by S-nitrosoglutathione reductase (GSNOR) that irreversibly inactivates the glutathione-bound NO to ammonium. Exogenous feeding of diverse RNS, including GSNO, affected chromatin accessibility and transcription of stress-related genes, but the triggering function of RNS on these regulatory processes remained elusive. Here, we show that GSNO reductase-deficient plants (gsnor1-3) accumulate S-adenosylmethionine (SAM), the principal methyl donor for methylation of DNA and histones. This SAM accumulation triggered a substantial increase in the methylation index (MI = [SAM]/[S-adenosylhomocysteine]), indicating the transmethylation activity and histone methylation status in higher eukaryotes. Indeed, a mass spectrometry-based global histone profiling approach demonstrated a significant global increase in H3K9me2, which was independently verified by immunological detection using a selective antibody. Since H3K9me2-modified regions tightly correlate with methylated DNA regions, we also determined the DNA methylation status of gsnor1-3 plants by whole-genome bisulfite sequencing. DNA methylation in the CG, CHG, and CHH contexts in gsnor1-3 was significantly enhanced compared to the wild type. We propose that GSNOR1 activity affects chromatin accessibility by controlling the transmethylation activity (MI) required for maintaining DNA methylation and the level of the repressive chromatin mark H3K9me2.

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Publication type Article: Journal article

Document type Scientific Article

Corresponding Author

Keywords Dna Methylation ; Histone Methylation ; Metaboloepigenetic ; Nitric Oxide ; S-adenosylhomocysteine ; S-nitrosoglutathione ; S-nitrosoglutathione Reductase; S-nitrosoglutathione Reductase; Nitric-oxide; Dna Methylation; Arabidopsis-thaliana; Nitrosylated Proteins; Jasmonoyl-isoleucine; Seed-germination; Mutant Deficient; Abscisic-acid; Rna-seq

ISSN (print) / ISBN 2076-3921

e-ISSN 2076-3921

Journal Antioxidants

Quellenangaben Volume: 10, Issue: 7, Article Number: 1128

Publisher MDPI

Publishing Place St Alban-anlage 66, Ch-4052 Basel, Switzerland

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Institute of Biochemical Plant Pathology (BIOP)

Grants Deutsche Forschungsgemeinschaft