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Home > Research > Publications & Outputs > 14-3-3 proteins and a 13-lipoxygenase form asso...
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14-3-3 proteins and a 13-lipoxygenase form associations in a phosphorylation-dependent manner.

Research output: Contribution to journalJournal article

Published

Journal publication date12/2000
JournalBiochemical Society Transactions
Journal number6
Volume28
Number of pages3
Pages834-836
Original languageEnglish

Abstract

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.