Sensing and signaling of oxidative stress in chloroplasts by inactivation of the SAL1 phosphoadenosine phosphatase
| Autor: | Jonathan W. Mueller, Nazia Nisar, Elke Stroeher, Peter D. Mabbitt, Barry J. Pogson, Julia Grassl, Su Yin Phua, Tamara Gigolashvili, Wiebke Arlt, Colin J. Jackson, Kai Xun Chan, Gonzalo M. Estavillo |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Chloroplasts Phosphatase Arabidopsis Biology medicine.disease_cause Substrate Specificity 03 medical and health sciences Gene Expression Regulation Plant medicine Arabidopsis thaliana Amino Acid Sequence Disulfides Plastid Multidisciplinary Sequence Homology Amino Acid Arabidopsis Proteins food and beverages biology.organism_classification Glutathione Phosphoric Monoester Hydrolases Adenosine Diphosphate Enzyme Activation Chloroplast Oxidative Stress 030104 developmental biology PNAS Plus Biochemistry Plant protein Retrograde signaling Protein Multimerization Oxidation-Reduction Oxidative stress Signal Transduction |
| Zdroj: | Proceedings of the National Academy of Sciences. 113 |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | Intracellular signaling during oxidative stress is complex, with organelle-to-nucleus retrograde communication pathways ill-defined or incomplete. Here we identify the 3'-phosphoadenosine 5'-phosphate (PAP) phosphatase SAL1 as a previously unidentified and conserved oxidative stress sensor in plant chloroplasts. Arabidopsis thaliana SAL1 (AtSAL1) senses changes in photosynthetic redox poise, hydrogen peroxide, and superoxide concentrations in chloroplasts via redox regulatory mechanisms. AtSAL1 phosphatase activity is suppressed by dimerization, intramolecular disulfide formation, and glutathionylation, allowing accumulation of its substrate, PAP, a chloroplast stress retrograde signal that regulates expression of plastid redox associated nuclear genes (PRANGs). This redox regulation of SAL1 for activation of chloroplast signaling is conserved in the plant kingdom, and the plant protein has evolved enhanced redox sensitivity compared with its yeast ortholog. Our results indicate that in addition to sulfur metabolism, SAL1 orthologs have evolved secondary functions in oxidative stress sensing in the plant kingdom. |
| Databáze: | OpenAIRE |
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