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

Juan C Moreno, Bruno E Rojas, Rubén Vicente, Michal Gorka, Timon Matz, Monika Chodasiewicz, Juan S Peralta-Ariza, Youjun Zhang, Saleh Alseekh, Dorothee Childs, Marcin Luzarowski, Zoran Nikoloski, Raz Zarivach, Dirk Walther, Matías D Hartman, Carlos M Figueroa, Alberto A Iglesias, Alisdair R. Fernie, Aleksandra Skirycz

Research output: Contribution to journalArticlepeer-review

Abstract

How organisms integrate metabolism with the external environ-ment is a central question in biology. Here, we describe a novelregulatory small molecule, a proteogenic dipeptide Tyr-Asp, whichimproves plant tolerance to oxidative stress by directly interferingwith glucose metabolism. Specifically, Tyr-Asp inhibits the activityof a key glycolytic enzyme, glyceraldehyde 3-phosphate dehydro-genase (GAPC), and redirects glucose toward pentose phosphatepathway (PPP) and NADPH production. In line with the metabolicdata, Tyr-Asp supplementation improved the growth performanceof both Arabidopsis and tobacco seedlings subjected to oxidativestress conditions. Moreover, inhibition of Arabidopsis phospho-enolpyruvate carboxykinase (PEPCK) activity by a group ofbranched-chain amino acid-containing dipeptides, but not by Tyr-Asp, points to a multisite regulation of glycolytic/gluconeogenicpathway by dipeptides. In summary, our results open the intrigu-ing possibility that proteogenic dipeptides act as evolutionarilyconserved small-molecule regulators at the nexus of stress, proteindegradation, and metabolism.
Original languageEnglish (US)
JournalThe EMBO Journal
DOIs
StatePublished - Jun 22 2021

ASJC Scopus subject areas

  • Neuroscience(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Molecular Biology
  • Immunology and Microbiology(all)

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