14-3-3 proteins interact with a 13-lipoxygenase, but not with a 9-lipoxygenase

• Published in: FEBS letters Vol. 474; no. 1; pp. 48 - 52
• Main Authors: Holtman, Wessel L., Roberts, Michael R., Oppedijk, Berry J., Testerink, Christa, van Zeijl, Mieke J., Wang, Mei
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 26-05-2000
• Subjects: 14-3-3 protein; 14-3-3 Proteins; Antibodies, Monoclonal; Chemical Phenomena; Chemistry, Physical; Escherichia coli; Hordeum - enzymology; Immunosorbent Techniques; Interaction; Isoenzymes - metabolism; Lipoxygenase; Lipoxygenase - chemistry; Lipoxygenase - metabolism; Lox, lipoxygenase; Proteins - chemistry; Proteins - metabolism; Recombinant Proteins - chemistry; Recombinant Proteins - metabolism; Surface Plasmon Resonance; Tyrosine 3-Monooxygenase; Lox, lipoxygenase; 14-3-3 protein; Lipoxygenase; Interaction
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(00)01575-1

Associations between lipoxygenases (Lox) and 14-3-3 proteins were demonstrated by two different methods. First, immunoprecipitation experiments, using isoenzyme-specific monoclonal Lox antibodies, showed that 14-3-3 proteins co-precipitate with 13-Lox, but not with the 9-Lox from barley. Second, interactions between 13-Lox and 14-3-3 were established by surface plasmon resonance studies, showing that 13-Lox binds with 14-3-3 proteins in a concentration-dependent manner. The interactions between 14-3-3 proteins and 13-Lox may reveal their role during plant development.