Pyrophosphate modulates plant stress responses via SUMOylation.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 30785397.
- Also identified by DOI 10.7554/eLife.44213 and PMC identifier 6382351.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Pyrophosphate (PPi), a byproduct of macromolecule biosynthesis is maintained at low levels by soluble inorganic pyrophosphatases (sPPase) found in all eukaryotes. In plants, H<sup>+</sup>-pumping pyrophosphatases (H<sup>+</sup>-PPase) convert the substantial energy present in PPi into an electrochemical gradient. We show here, that both cold- and heat stress sensitivity of <i>fugu5</i> mutants lacking the major H<sup>+</sup>-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.
Medical subject headings
- Arabidopsis
- Diphosphates
- Stress, Physiological
- Sumoylation