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

Author: Holtman, W.L. · Roberts, M.R. · Oppedijk, B.J. · Testerink, C. · Zeijl, M.J. van · Wang, M.
Type:article
Date:2000
Source:FEBS Letters, 1, 474, 48-52
Identifier: 235560
doi: doi:10.1016/S0014-5793(00)01575-1
Keywords: Interaction · 13 lipoxygenase · 9 lipoxygenase · lipoxygenase · unclassified drug · barley · enzyme purification · enzyme substrate complex · germination · immunoprecipitation · nucleotide sequence · protein family · protein phosphorylation · surface plasmon resonance · Western blotting · 14-3-3 Proteins · Antibodies, Monoclonal · Chemistry, Physical · Escherichia coli · Hordeum · Immunosorbent Techniques · Isoenzymes · Lipoxygenase · Proteins · Recombinant Proteins · Surface Plasmon Resonance · Tyrosine 3-Monooxygenase · Hordeum vulgare subsp. vulgare

Abstract

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. Copyright (C) 2000 Federation of European Biochemical Societies. Molecular Sequence Numbers: GENBANK: L35931, L37358, X62388, X93170, Y14200; Chemicals/CAS: 13-lipoxygenase, EC 1.13.11.-; 14-3-3 Proteins; Antibodies, Monoclonal; Isoenzymes; Lipoxygenase, EC 1.13.11.12; Proteins; Recombinant Proteins; Tyrosine 3-Monooxygenase, EC 1.14.16.2