14-3-3 Proteins and a 13-lipoxygenase form associations in a phosphorylation-dependent manner
article
Recently, we have demonstrated by two different methods that lipoxgenases (LOXs) and 14-3-3 proteins form interactions in barley embryos [Holtman, Roberts, Oppedijk, Testerink, van Zeijl and Wang (2000) FEBS Lett. 474, 48-52]. It was shown by both co-immunoprecipitations and surface-plasmon resonance experiments that 13-LOX, but not 9-LOX, forms interactions with 14-3-3 proteins. In the present report we show that the presence of 13-LOX and 14-3-3 proteins was established in high-molecular-mass complexes. Amounts of 13-LOX and 14-3-3 proteins in high-molecular-mass fractions increased during germination, but were reduced after dephosphorylation of protein extracts or competition with the 14-3-3-binding peptide P-Raf-259, indicating that 13-LOX and 14-3-3 proteins interact in a phosphorylation-dependent manner.
Chemicals/CAS: 13-lipoxygenase, EC 1.13.11.-; 14-3-3 Proteins; Lipoxygenase, EC 1.13.11.12; Tyrosine 3-Monooxygenase, EC 1.14.16.2
Chemicals/CAS: 13-lipoxygenase, EC 1.13.11.-; 14-3-3 Proteins; Lipoxygenase, EC 1.13.11.12; Tyrosine 3-Monooxygenase, EC 1.14.16.2
Topics
Lipid metabolismProtein interactionslipoxygenaseM proteinBarleyConference paperDephosphorylationEmbryoGel filtrationGerminationMolecular weightPriority journalProtein interactionProtein phosphorylationReversed phase high performance liquid chromatographySurface plasmon resonance14-3-3 ProteinsBlotting, WesternChromatography, GelElectrophoresis, Polyacrylamide GelHordeumLipoxygenasePhosphorylationProtein BindingSeedsTyrosine 3-MonooxygenaseHordeum vulgare subsp. vulgare
TNO Identifier
57048
Source
Biochemical Society Transactions, 28(6), pp. 834-836.
Pages
834-836
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