Pyrophosphate modulates plant stress responses via SUMOylation

ELife
M Görkem Patir-NebiogluKarin Schumacher

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+-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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Datasets Mentioned

BETA
ABIN459215
AB113687

Methods Mentioned

BETA
transgenic
ubiquitination
FRET
sumoylation
gel filtration
PCR
Fluorescence
chip

Software Mentioned

Leica Application Suite Advanced Fluorescence
Fiji
Origin
ImageJ

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