Tyr‐Asp inhibition of glyceraldehyde 3‐phosphate dehydrogenase affects plant redox metabolism

MORENO, JUAN C; ROJAS, BRUNO E; VICENTE, RUBÉN; GORKA, MICHAL; MATZ, TIMON; CHODASIEWICZ, MONIKA; PERALTA?ARIZA, JUAN S; ZHANG, YOUJUN; ALSEEKH, SALEH; CHILDS, DOROTHEE; LUZAROWSKI, MARCIN; NIKOLOSKI, ZORAN; ZARIVACH, RAZ; WALTHER, DIRK; HARTMAN, MATÍAS D; FIGUEROA, CARLOS M; IGLESIAS, ALBERTO A; FERNIE, ALISDAIR R; SKIRYCZ, ALEKSANDRA

EMBO JOURNAL

NATURE PUBLISHING GROUP

Lugar: Londres; Año: 2021 vol. 40

0261-4189

How organisms integrate metabolism with the external environment is a central question in biology. Here, we describe a novel regulatory small molecule, a proteogenic dipeptide Tyr-Asp, which improves plant tolerance to oxidative stress by directly interfering with glucose metabolism. Specifically, Tyr-Asp inhibits the activity of a key glycolytic enzyme, glyceraldehyde 3-phosphate dehydrogenase (GAPC), and redirects glucose toward pentose phosphate pathway (PPP) and NADPH production. In line with the metabolic data, Tyr-Asp supplementation improved the growth performance of both Arabidopsis and tobacco seedlings subjected to oxidative stress conditions. Moreover, inhibition of Arabidopsis phosphoenolpyruvate carboxykinase (PEPCK) activity by a group of branched-chain amino acid-containing dipeptides, but not by Tyr-Asp, points to a multisite regulation of glycolytic/gluconeogenic pathway by dipeptides. In summary, our results open the intriguing possibility that proteogenic dipeptides act as evolutionarily conserved small-molecule regulators at the nexus of stress, protein degradation, and metabolism.