{"doi":"10.1111/pce.70423","title":"A Coupled GSH/GSNOR System Denitrosylates TRXh5 to Allow Activation of SA Signalling by Oxidative Stress","abstract":"<jats:title>ABSTRACT</jats:title>\n                  <jats:p>\n                    Accumulating evidence shows that reversible protein\n                    <jats:italic>S</jats:italic>\n                    ‐nitrosylation is essential for H\n                    <jats:sub>2</jats:sub>\n                    O\n                    <jats:sub>2</jats:sub>\n                    homoeostasis and signalling. 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‐defective 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‐induced 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                    ‐triggered SA responses. Intriguingly, TRX\n                    <jats:italic>h5</jats:italic>\n                    ‐reinforced SA responses were antagonised by glutathione (GSH) deficiency when introducing additional\n                    <jats:italic>pad2</jats:italic>\n                    mutation, localised in the GLUTAMATE‐CYSTEINE 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‐SNO formation in\n                    <jats:italic>TRXH5‐YFP cat2 pad2 trxh5</jats:italic>\n                    than in\n                    <jats:italic>TRXH5‐YFP cat2 trxh5</jats:italic>\n                    . Furthermore,\n                    <jats:italic>S</jats:italic>\n                    ‐nitrosoglutathione reductase (GSNOR) was capable of physically interacting with TRX\n                    <jats:italic>h</jats:italic>\n                    5, and was also required for GSH‐dependent TRX\n                    <jats:italic>h</jats:italic>\n                    5 denitrosylation and TRX\n                    <jats:italic>h</jats:italic>\n                    5‐enhanced SA responses during oxidative stress. Collectively, these data suggest that GSH/GSNOR constitutes an active denitrosylating module that works together with the canonical NADPH‐dependent TRX‐reducing pathway to sustain cytosolic TRX\n                    <jats:italic>h</jats:italic>\n                    5 operation within the oxidative signalling framework.\n                  </jats:p>","journal":"Plant, Cell &amp; Environment","year":2026,"id":677463,"datarank":0.20794415416798362,"base_score":1.3862943611198906,"endowment":1.3862943611198906,"self_citation_contribution":0.20794415416798362,"citation_network_contribution":0.0,"self_endowment_contribution":0.20794415416798362,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":3,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1770116,"name":"Shengchun Li","orcid":"0000-0003-2930-844X","position":1,"is_corresponding":false},{"id":1770118,"name":"Xiujie Mu","orcid":null,"position":2,"is_corresponding":false},{"id":1770122,"name":"Tianzhao Yang","orcid":null,"position":3,"is_corresponding":false},{"id":720958,"name":"Lijuan Wang","orcid":"0000-0001-5944-3453","position":4,"is_corresponding":false},{"id":1770126,"name":"Mimi Tian","orcid":null,"position":5,"is_corresponding":false},{"id":295121,"name":"Mei Yu","orcid":"0000-0002-2140-8756","position":6,"is_corresponding":false},{"id":853079,"name":"Long Luo","orcid":"0000-0001-5771-6892","position":7,"is_corresponding":false},{"id":1770130,"name":"Yuanming Xie","orcid":null,"position":8,"is_corresponding":false},{"id":318364,"name":"Wei Xuan","orcid":"0000-0002-4859-2637","position":9,"is_corresponding":false},{"id":1770134,"name":"Graham Noctor","orcid":null,"position":10,"is_corresponding":false},{"id":1235246,"name":"Yi Han","orcid":"0000-0002-4424-1485","position":11,"is_corresponding":false},{"id":961187,"name":"Tao Chen","orcid":"0000-0002-2147-709X","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"A Coupled GSH/GSNOR System Denitrosylates TRXh5 to Allow Activation of SA Signalling by Oxidative Stress","abstract":"<jats:title>ABSTRACT</jats:title>\n                  <jats:p>\n                    Accumulating evidence shows that reversible protein\n                    <jats:italic>S</jats:italic>\n                    ‐nitrosylation is essential for H\n                    <jats:sub>2</jats:sub>\n                    O\n                    <jats:sub>2</jats:sub>\n                    homoeostasis and signalling. 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‐defective 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‐induced 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                    ‐triggered SA responses. Intriguingly, TRX\n                    <jats:italic>h5</jats:italic>\n                    ‐reinforced SA responses were antagonised by glutathione (GSH) deficiency when introducing additional\n                    <jats:italic>pad2</jats:italic>\n                    mutation, localised in the GLUTAMATE‐CYSTEINE 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‐SNO formation in\n                    <jats:italic>TRXH5‐YFP cat2 pad2 trxh5</jats:italic>\n                    than in\n                    <jats:italic>TRXH5‐YFP cat2 trxh5</jats:italic>\n                    . Furthermore,\n                    <jats:italic>S</jats:italic>\n                    ‐nitrosoglutathione reductase (GSNOR) was capable of physically interacting with TRX\n                    <jats:italic>h</jats:italic>\n                    5, and was also required for GSH‐dependent TRX\n                    <jats:italic>h</jats:italic>\n                    5 denitrosylation and TRX\n                    <jats:italic>h</jats:italic>\n                    5‐enhanced SA responses during oxidative stress. Collectively, these data suggest that GSH/GSNOR constitutes an active denitrosylating module that works together with the canonical NADPH‐dependent TRX‐reducing pathway to sustain cytosolic TRX\n                    <jats:italic>h</jats:italic>\n                    5 operation within the oxidative signalling framework.\n                  </jats:p>","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"41611640","pmcid":null,"openalex_id":null,"authors":[],"funders":[{"funder_name":"Natural Science Foundation of Anhui Province","grant_id":"2208085MC44","title":null},{"funder_name":"French Agence Nationale de la Recherche HIPATH project","grant_id":"ANR-17-CE20- 0025","title":null},{"funder_name":"National Natural Science Foundation","grant_id":"32402662","title":null},{"funder_name":"Natural Science Research Project of Anhui Educational Committee","grant_id":"2024AH050427","title":null}],"total_grants":4,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":null,"license":"http://doi.wiley.com/10.1002/tdm_license_1.1","oa_locations":[{"url":"https://onlinelibrary.wiley.com/doi/pdf/10.1111/pce.70423","host_type":"publisher"},{"url":"https://onlinelibrary.wiley.com/doi/full-xml/10.1111/pce.70423","host_type":"publisher"}],"fields_of_study":[],"mesh_terms":["Arabidopsis","Hydrogen Peroxide","Salicylic Acid","Aldehyde Oxidoreductases","Glutathione Reductase","Catalase","Glutathione","Arabidopsis Proteins","Signal Transduction","Oxidative Stress","Thioredoxins"],"keywords":["Nitric oxide","Glutathione","Hydrogen peroxide","Oxidative stress","S‐nitrosylation/denitrosylation"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-17T04:10:09.105816Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}