PXD019332 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Dipeptide Tyr-Asp inhibits glyceraldehyde 3-phosphate dehydrogenase activity, affecting redox metabolism and boosting plant stress resistance. |
Description | Proteogenic dipeptides are not only intermediates of proteolysis but also an emerging class of small molecule regulators, with diverse and specific functions. We have recently reported a novel in vitro interaction between the dipeptide Tyr-Asp and the Arabidopsis glycolytic enzyme glyceraldehyde 3- phosphate dehydrogenase (GAPDH). To understand the functional significance of Tyr-Asp/GAPDH binding, we examined the effect produced on the enzymatic activity. Results demonstrate that low to mid micro-molar concentrations of Tyr-Asp, but none of the other tested dipeptides, inhibit GAPDH activity both in vitro and in planta. Inhibition of the GAPDH activity was associated with a shift of the flux from glycolysis towards the pentose phosphate pathway and an increase in the NADPH/NADP+ ratio, a known response to cope with oxidative stress. In addition to GAPDH, the Tyr-Asp protein interactome comprised further stress-related proteins, including multiple chaperones. In line with the molecular data, Tyr-Asp supplementation improved growth performance of both Arabidopsis and tobacco seedlings subjected to oxidative stress conditions. By contrast, no such improvement was measured, neither for the free amino acids nor the other tested dipeptides, demonstrating that the action of Tyr-Asp is specific and independent of the degradation of Tyr-Asp to the constituent amino acids. Finally, inhibition of Arabidopsis phosphoenolpyruvate carboxykinase activity reveals a multisite regulation of glycolytic/gluconeogenic flux by dipeptides. In summary, our data suggest proteogenic dipeptides as a novel class of small-molecule regulators operating at the nexus of stress, protein degradation and metabolism. |
HostingRepository | PRIDE |
AnnounceDate | 2021-05-10 |
AnnouncementXML | Submission_2021-05-10_03:23:23.468.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Michal Gorka |
SpeciesList | scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702; |
ModificationList | iodoacetamide derivatized residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2020-05-21 17:55:13 | ID requested | |
⏵ 1 | 2021-05-10 03:23:23 | announced | |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: Arabidopsis, dipeptides, GAPDH, glycolysis, Tyr-Asp, oxidative stress, PEPCK |
Contact List
Aleksandra Skirzcy |
contact affiliation | Dr. Aleksandra Skirycz Max-Planck-Institut für Molekulare Pflanzenphysiologie Potsdam Science Park Am Mühlenberg 1 14476 Potsdam |
contact email | skirycz@mpimp-golm.mpg.de |
lab head | |
Michal Gorka |
contact affiliation | Max Planck Institute for Molecular Plant Physiology |
contact email | gorka@mpimp-golm.mpg.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD019332
- Label: PRIDE project
- Name: Dipeptide Tyr-Asp inhibits glyceraldehyde 3-phosphate dehydrogenase activity, affecting redox metabolism and boosting plant stress resistance.