Pyrophosphate modulates plant stress responses via SUMOylation
Pyrophosphate (PPi), a byproduct of macromolecule biosynthesis is maintained at low levels by soluble inorganic pyrophosphatases (sPPase) found in all eukaryotes. In plants, H+-pumping pyrophosphatases (H+-PPase) convert the substantial energy present in PPi into an electrochemical gradient. We show...
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| Hauptverfasser: | , , , , , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
Feb. 20, 2019
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| In: |
eLife
Year: 2019, Jahrgang: 8, Pages: 1-23 |
| ISSN: | 2050-084X |
| DOI: | 10.7554/eLife.44213 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.7554/eLife.44213
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| Verfasserangaben: | M Görkem Patir-Nebioglu, Zaida Andrés, Melanie Krebs, Fabian Fink, Katarzyna Drzewicka, Nicolas Stankovic-Valentin, Shoji Segami, Sebastian Schuck, Michael Büttner, Rüdiger Hell, Masayoshi Maeshima, Frauke Melchior, Karin Schumacher |
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| 520 | |a Pyrophosphate (PPi), a byproduct of macromolecule biosynthesis is maintained at low levels by soluble inorganic pyrophosphatases (sPPase) found in all eukaryotes. In plants, H+-pumping pyrophosphatases (H+-PPase) convert the substantial energy present in PPi into an electrochemical gradient. We show here, that both cold- and heat stress sensitivity of fugu5 mutants lacking the major H+-PPase isoform AVP1 is correlated with reduced SUMOylation. In addition, we show that increased PPi concentrations interfere with SUMOylation in yeast and we provide evidence that SUMO activating E1-enzymes are inhibited by micromolar concentrations of PPi in a non-competitive manner. Taken together, our results do not only provide a mechanistic explanation for the beneficial effects of AVP1 overexpression in plants but they also highlight PPi as an important integrator of metabolism and stress tolerance. | ||
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