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 Zeij] 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.
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Conference Article|
December 01 2000
14-3-3 Proteins and a 13-lipoxygenase form associations in a phosphorylation-dependent manner
W. L. Holtman;
W. L. Holtman
1
*Center for Phytotechnology UL-TNO, Department of Applied Plant Sciences, Wassenaarseweg 64, 2333 AL Leiden, The Netherlands
1To whom correspondence should be addressed (e-mail holtman@voeding.tno.nl)
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M. R. Roberts;
M. R. Roberts
†The Plant Laboratory, Department of Biology, University of York, Heslington, York Y010 5DD, U.K.
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M. Wang
M. Wang
*Center for Phytotechnology UL-TNO, Department of Applied Plant Sciences, Wassenaarseweg 64, 2333 AL Leiden, The Netherlands
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Publisher: Portland Press Ltd
Received:
June 26 2000
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2000 Biochemical Society
2000
Biochem Soc Trans (2000) 28 (6): 834–836.
Article history
Received:
June 26 2000
Citation
W. L. Holtman, M. R. Roberts, M. Wang; 14-3-3 Proteins and a 13-lipoxygenase form associations in a phosphorylation-dependent manner. Biochem Soc Trans 1 December 2000; 28 (6): 834–836. doi: https://doi.org/10.1042/bst0280834
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