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14-3-3 Proteins and a 13-lipoxygenase form associations in a phosphorylation-dependent manner

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Author: Holtman, W.L. · Roberts, M.R. · Wang, M.
Source:Biochemical Society Transactions, 6, 28, 834-836
Identifier: 57048
Keywords: Lipid metabolism · Protein interactions · lipoxygenase · M protein · barley · conference paper · dephosphorylation · embryo · gel filtration · germination · molecular weight · priority journal · protein interaction · protein phosphorylation · reversed phase high performance liquid chromatography · surface plasmon resonance · 14-3-3 Proteins · Blotting, Western · Chromatography, Gel · Electrophoresis, Polyacrylamide Gel · Hordeum · Lipoxygenase · Phosphorylation · Protein Binding · Seeds · Tyrosine 3-Monooxygenase · Hordeum vulgare subsp. vulgare


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; Tyrosine 3-Monooxygenase, EC