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

Full text not available from this repository.

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:
Journal Article
Journal or Publication Title:
Biochemical Society Transactions
Uncontrolled Keywords:
/dk/atira/pure/researchoutput/libraryofcongress/qh301
Subjects:
ID Code:
9487
Deposited By:
Deposited On:
11 Jun 2008 15:47
Refereed?:
Yes
Published?:
Published
Last Modified:
22 Apr 2020 01:56