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Accumulation of endogenous peptides triggers a pathogen stress response in Arabidopsis thaliana
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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Number of Authors: 102018 (English)In: The Plant Journal, ISSN 0960-7412, E-ISSN 1365-313X, Vol. 96, no 4, p. 705-715Article in journal (Refereed) Published
Abstract [en]

The stepwise degradation of peptides to amino acids in plant mitochondria and chloroplasts is catalyzed by a network of oligopeptidases (presequence protease PreP, organellar oligopeptidase OOP) and aminopeptidases. In the present report, we show that the lack of oligopeptidase activity in Arabidopsis thaliana results in the accumulation of endogenous free peptides, mostly of chloroplastic origin (targeting peptides and degradation products). Using mRNA sequencing and deep coverage proteomics, allowing for the identification of 17 000 transcripts and 11 000 proteins, respectively, we uncover a peptide-stress response occurring in plants lacking PreP and OOP oligopeptidase activity. The peptide-stress response results in the activation of the classical plant defense pathways in the absence of pathogenic challenge. The constitutive activation of the pathogen-defense pathways imposes a strong growth penalty and a reduction of the plants reproductive fitness. Our results indicate that the absence of organellar oligopeptidases PreP1/2 and OOP results in the accumulation of peptides that are perceived as pathogenic effectors and activate the signaling pathways of plant-defense response.

Place, publisher, year, edition, pages
2018. Vol. 96, no 4, p. 705-715
Keywords [en]
chloroplasts, oligopeptidase, peptides, peptide degradation, defense response
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-162996DOI: 10.1111/tpj.14100ISI: 000449986700002PubMedID: 30242930OAI: oai:DiVA.org:su-162996DiVA, id: diva2:1270217
Available from: 2018-12-12 Created: 2018-12-12 Last updated: 2018-12-12Bibliographically approved

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Kmiec, BeataGlaser, ElzbietaTeixeira, Pedro F.
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