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Tyr‐Asp inhibition of glyceraldehyde 3‐phosphate dehydrogenase affects plant redox metabolism
Author(s) -
Moreno Juan C,
Rojas Bruno E,
Vicente Rubén,
Gorka Michal,
Matz Timon,
Chodasiewicz Monika,
PeraltaAriza 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
Publication year - 2021
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.2020106800
Subject(s) - pentose phosphate pathway , biochemistry , phosphoenolpyruvate carboxykinase , glycolysis , arabidopsis , glyceraldehyde 3 phosphate dehydrogenase , dehydrogenase , metabolism , biology , chemistry , enzyme , gene , mutant
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.