Moonlighting Function of Phytochelatin Synthase1 in Extracellular Defense against Fungal Pathogens
العنوان: | Moonlighting Function of Phytochelatin Synthase1 in Extracellular Defense against Fungal Pathogens |
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المؤلفون: | Melisa Lim, Mariola Piślewska-Bednarek, Rene Fuchs, Volker Lipka, Kian Hématy, Paweł Bednarek, Shauna Somerville, Clara Sánchez-Rodríguez, Candice Cherk, Erwin Grill, Paul Schulze-Lefert, Mónica Stein, Antonio Molina, Christine Klapprodt |
المساهمون: | Carnegie Institution for Science, Department of Plant Biology, Stanford University-Stanford University, Energy Biosciences Institute, University of California [Berkeley], University of California-University of California, Department of Plant Microbe Interactions, Max Planck Institute for Plant Breeding Research (MPIPZ), Institute of Bioorganic Chemistry, Polish Academy of Sciences (PAN), Centro de Biotecnología y Genómica de Plantas, Universidad Politécnica de Madrid-Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA), Schwann-Schleiden Research Center for Molecular Cell Biology, University Medical Center Göttingen (UMG), Departamento de Biotecnología-Biología Vegetal, Escuela Técnica Superior de Ingeniería Agronómica, Alimentaria y de Biosistemas, Lehrstuhl für Botanik, Technische Universtät München, National Science Foundation (NSF) Carnegie Institution for Science Stanford University Max Planck SocietyFoundation CELLEX German Research Foundation (DFG)SPP1212GR 938LI 1317/2-1Spanish Ministry of Economy and Competitiveness (MINECO) BIO2015-64077-RBIO2012-32910Polish National Science Centre 2012/07/E/NZ2/04098 |
المصدر: | Plant Physiology Plant Physiology, American Society of Plant Biologists, 2020, 182 (4), pp.1920-1932. ⟨10.1104/pp.19.01393⟩ |
بيانات النشر: | HAL CCSD, 2020. |
سنة النشر: | 2020 |
مصطلحات موضوعية: | 0106 biological sciences, Protein moonlighting, Physiology, [SDV]Life Sciences [q-bio], Mutant, Arabidopsis, Plant Science, 01 natural sciences, Catalysis, chemistry.chemical_compound, Arabidopsis-thaliana, Ascomycota, Gene Expression Regulation, Plant, Phytochelatins, Genetics, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, Research Articles, Heavy metal detoxification, Glucosinolate Metabolism, biology, Arabidopsis Proteins, Myrosinase, Binding Cassette Transporter, Nonhost Resistance, Tryptophan, Glutathione, Plants, Genetically Modified, biology.organism_classification, Mitochondria, Metabolic pathway, Biochemistry, chemistry, Gamma-glutamylcysteine, Phytochelatin, Pathogens, Tolerance, 010606 plant biology & botany |
الوصف: | Phytochelatin synthase (PCS) is a key component of heavy metal detoxification in plants. PCS catalyzes both the synthesis of the peptide phytochelatin from glutathione and the degradation of glutathione conjugates via peptidase activity. Here, we describe a role for PCS in disease resistance against plant pathogenic fungi. The pen4 mutant, which is allelic to cadmium insensitive1 (cad1/pcs1) mutants, was recovered from a screen for Arabidopsis mutants with reduced resistance to the nonadapted barley fungal pathogen Blumeria graminis f. sp. hordei. PCS1, which is found in the cytoplasm of cells of healthy plants, translocates upon pathogen attack and colocalizes with the PEN2 myrosinase on the surface of immobilized mitochondria. pcs1 and pen2 mutant plants exhibit similar metabolic defects in the accumulation of pathogen-inducible indole glucosinolate-derived compounds, suggesting that PEN2 and PCS1 act in the same metabolic pathway. The function of PCS1 in this pathway is independent of phytochelatin synthesis and deglycination of glutathione conjugates, as catalytic-site mutants of PCS1 are still functional in indole glucosinolate metabolism. In uncovering a peptidase-independent function for PCS1, we reveal this enzyme to be a moonlighting protein important for plant responses to both biotic and abiotic stresses. |
وصف الملف: | application/pdf |
اللغة: | English |
تدمد: | 0032-0889 1532-2548 |
DOI: | 10.1104/pp.19.01393⟩ |
URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c03772d662c2a4abb16b706f740feaf https://hal.inrae.fr/hal-02995321 |
Rights: | OPEN |
رقم الانضمام: | edsair.doi.dedup.....3c03772d662c2a4abb16b706f740feaf |
قاعدة البيانات: | OpenAIRE |
تدمد: | 00320889 15322548 |
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DOI: | 10.1104/pp.19.01393⟩ |