RT Journal Article
SR Electronic
T1 Pyrophosphate modulates stress responses via SUMOylation
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 504373
DO 10.1101/504373
A1 M. Görkem Patir-Nebioglu
A1 Zaida Andrés
A1 Melanie Krebs
A1 Fabian Fink
A1 Katarzyna Drzewicka
A1 Nicolas Stankovic-Valentin
A1 Shoji Segami
A1 Sebastian Schuck
A1 Michael Büttner
A1 Rüdiger Hell
A1 Masayoshi Maeshima
A1 Frauke Melchior
A1 Karin Schumacher
YR 2018
UL http://biorxiv.org/content/early/2018/12/22/504373.abstract
AB 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 caused by 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.