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Effects of Erysiphe pisi on protein profiles and ribulose-1,5-bisphosphate carboxylase content in resistant and susceptible pea (Pisum sativum × Pisum fulvum) plants

Einfluss von Erysiphe pisi auf Proteinprofile und den Ribulose-1,5-bisphosphatcarboxylase-Gehalt in resistenten und anfälligen Erbsenpflanzen (Pisum sativum × Pisum fulvum)

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Abstract

The fate of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) was examined in leaves of both resistant and susceptible plants from a Pisum sativum × Pisum fulvum cross after challenge with Erysiphe pisi. High performance liquid chromatography and 1-dimensional gel electrophoresis revealed a 51 kDa protein that was much more abundant in leaves of resistant versus susceptible plants, and which was identified as the Rubisco large chain precursor by mass spectrometry. Greater quantities of Rubisco in resistant tissue suggested that the protein may serve as an important nutrient source for E. pisi in infected susceptible leaves. Liquid chromatography — tandem mass spectrometry revealed three defense-response proteins only in extracts from resistant tissue, while proteins similar to the antimicrobial peptides viscotoxin and phoratoxin from mistletoes, and bubble protein from the yeast Williopsis mrakii, were found only in susceptible tissue. Greater numbers of DNA synthesis and regulation proteins were also identified in the susceptible vs. resistant tissue, probably resulting from changes in host metabolism induced by E. pisi.

Zusammenfassung

Der Gehalt an Ribulose-1,5-bisphosphatcarboxylase/oxygenase (Rubisco) wurde in Blättern resistenter und anfälliger Pflanzen aus einer Kreuzung von Pisum sativum × Pisum fulvum nach der Inokulation mit Erysiphe pisi untersucht. Hochdruckflüssigkeitschromatographie und eindimensionale Gelelektrophorese zeigten, dass ein 51-kDa-Protein sehr viel häufiger in resistenten Pflanzen als in anfälligen vertreten war, und dieses Protein wurde als Vorstufe der großen Untereinheit der Rubisco mittels Massenspektrometrie identifiziert. Die höheren Rubisco-Gehalte resistenter Pflanzengewebe deuten an, dass dieses Protein als eine wichtige Nährstoffquelle für E. pisi in anfälligen Blättern dienen könnte. Flüssigkeitschromatographie-Tandemmassenspektrometrie zeigte drei Abwehrproteine ausschließlich in resistenten Pflanzengeweben. Den antimikrobiellen Peptiden Viscotoxin und Phoratoxin aus Misteln sowie dem Bubble-Protein aus der Hefe Williopsis mrakii ähnliche Proteine wurden dagegen nur in Geweben anfälliger Pflanzen gefunden. Die Anzahl bei der DNA-Synthese und — Regulation wirkender Proteine war in anfälligen Geweben ebenfalls höher als in resistenten, was wahrscheinlich auch aus der Beeinflussung des Wirtsstoffwechsels durch E. pisi resultiert.

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Hwang, S.F., Zhang, X.R., Strelkov, S.E. et al. Effects of Erysiphe pisi on protein profiles and ribulose-1,5-bisphosphate carboxylase content in resistant and susceptible pea (Pisum sativum × Pisum fulvum) plants. J Plant Dis Prot 117, 15–23 (2010). https://doi.org/10.1007/BF03356328

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