14-3-3 proteins and a 13-lipoxygenase form associations in a phosphorylation-dependent manner.
Biochem Soc Trans
; 28(6): 834-6, 2000 Dec.
Article
en En
| MEDLINE
| ID: mdl-11171225
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Tirosina 3-Monooxigenasa
/
Hordeum
/
Lipooxigenasa
Tipo de estudio:
Risk_factors_studies
Idioma:
En
Revista:
Biochem Soc Trans
Año:
2000
Tipo del documento:
Article
País de afiliación:
Países Bajos
Pais de publicación:
Reino Unido