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

Holtman, W. L. and Roberts, Michael R. and Wang, Mei (2000) 14-3-3 proteins and a 13-lipoxygenase form associations in a phosphorylation-dependent manner. Biochemical Society Transactions, 28 (6). pp. 834-836. ISSN 0300-5127

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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.

Item Type: Article
Journal or Publication Title: Biochemical Society Transactions
Uncontrolled Keywords: lipid metabolism ; protein interactions.
Subjects: Q Science > QH Natural history > QH301 Biology
Departments: Faculty of Science and Technology > Lancaster Environment Centre
ID Code: 9487
Deposited By: Dr Michael R Roberts
Deposited On: 11 Jun 2008 16:47
Refereed?: Yes
Published?: Published
Last Modified: 24 Sep 2012 16:56
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/9487

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