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However, roles for denitrosylation in such oxidative signalling remain poorly understood. Here, we examined this question using the\n                    <jats:italic>Arabidopsis<\/jats:italic>\n                    catalase\u2010defective mutant,\n                    <jats:italic>cat2<\/jats:italic>\n                    , in which oxidative stress induces both glutathione accumulation and salicylic acid (SA) pathways. Induction of these pathways was accompanied by enhanced thioredoxin (\n                    <jats:italic>TRXH5<\/jats:italic>\n                    ) expression, and oxidative stress\u2010induced activation of the SA pathway was compromised when\n                    <jats:italic>TRXH5<\/jats:italic>\n                    expression was genetically disabled, whereas\n                    <jats:italic>TRXH5<\/jats:italic>\n                    overexpression stimulates H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    \u2010triggered SA responses. Intriguingly, TRX\n                    <jats:italic>h5<\/jats:italic>\n                    \u2010reinforced SA responses were antagonised by glutathione (GSH) deficiency when introducing additional\n                    <jats:italic>pad2<\/jats:italic>\n                    mutation, localised in the GLUTAMATE\u2010CYSTEINE LIGASE gene encoding the first enzyme of glutathione biosynthesis. Further analysis revealed that the two active cysteine residues of recombinant TRX\n                    <jats:italic>h<\/jats:italic>\n                    5 can be denitrosylated by GSH. Blocking glutathione accumulation increased more TRX\n                    <jats:italic>h<\/jats:italic>\n                    5\u2010SNO formation in\n                    <jats:italic>TRXH5\u2010YFP cat2 pad2 trxh5<\/jats:italic>\n                    than in\n                    <jats:italic>TRXH5\u2010YFP cat2 trxh5<\/jats:italic>\n                    . Furthermore,\n                    <jats:italic>S<\/jats:italic>\n                    \u2010nitrosoglutathione reductase (GSNOR) was capable of physically interacting with TRX\n                    <jats:italic>h<\/jats:italic>\n                    5, and was also required for GSH\u2010dependent TRX\n                    <jats:italic>h<\/jats:italic>\n                    5 denitrosylation and TRX\n                    <jats:italic>h<\/jats:italic>\n                    5\u2010enhanced SA responses during oxidative stress. Collectively, these data suggest that GSH\/GSNOR constitutes an active denitrosylating module that works together with the canonical NADPH\u2010dependent TRX\u2010reducing pathway to sustain cytosolic TRX\n                    <jats:italic>h<\/jats:italic>\n                    5 operation within the oxidative signalling framework.\n                  <\/jats:p>","DOI":"10.1111\/pce.70423","type":"journal-article","created":{"date-parts":[[2026,1,30]],"date-time":"2026-01-30T03:34:25Z","timestamp":1769744065000},"page":"2691-2705","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["A Coupled GSH\/GSNOR System Denitrosylates TRXh5 to Allow Activation of SA Signalling by Oxidative Stress"],"prefix":"10.1111","volume":"49","author":[{"given":"Tao","family":"Chen","sequence":"first","affiliation":[{"name":"Bio\u2010Breeding Laboratory of Anhui Province, School of Life Sciences Anhui Agricultural University Hefei China"},{"name":"Institute of Plant Sciences Paris Saclay IPS2, Universit\u00e9 Paris\u2010Sud, CNRS, INRA, Universit\u00e9 Evry, Paris Diderot, Sorbonne Paris\u2010Cit\u00e9, Universit\u00e9 Paris\u2010Saclay Orsay France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2930-844X","authenticated-orcid":false,"given":"Shengchun","family":"Li","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Biocatalysis and Enzyme Engineering, School of Life Sciences Hubei University Wuhan China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiujie","family":"Mu","sequence":"additional","affiliation":[{"name":"School of Food and Biological Engineering Hefei University of Technology Hefei China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tianzhao","family":"Yang","sequence":"additional","affiliation":[{"name":"Bio\u2010Breeding Laboratory of Anhui Province, School of Life Sciences Anhui Agricultural University Hefei China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lijuan","family":"Wang","sequence":"additional","affiliation":[{"name":"Bio\u2010Breeding Laboratory of Anhui Province, School of Life Sciences Anhui Agricultural University Hefei China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mimi","family":"Tian","sequence":"additional","affiliation":[{"name":"School of Food and Biological Engineering Hefei University of Technology Hefei China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mei","family":"Yu","sequence":"additional","affiliation":[{"name":"Bio\u2010Breeding Laboratory of Anhui Province, School of Life Sciences Anhui Agricultural University Hefei China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Long","family":"Luo","sequence":"additional","affiliation":[{"name":"Bio\u2010Breeding Laboratory of Anhui Province, School of Life Sciences Anhui Agricultural University Hefei 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