Detection of Ca2+-Dependent Transglutaminase Activity in Root and Leaf Tissue of Monocotyledonous and Dicotyledonous Plants

AUTOR(ES)

Lilley, Graham R.

FONTE

American Society of Plant Physiologists

RESUMO

Protein extracted from root and leaf tissue of the dicotyledonous plants pea (Pisum sativum) and broad bean (Vicia faba) and the monocotyledonous plants wheat (Triticum aestivum) and barley (Hordeum vulgare) were shown to catalyze the incorporation of biotin-labeled cadaverine into microtiter-plate-bound N′,N′-dimethylcasein and the cross-linking of biotin-labeled casein to microtiter-plate-bound casein in a Ca2+-dependent manner. The cross-linking of biotinylated casein and the incorporation of biotin-labeled cadaverine into N′,N′-dimethylcasein were time-dependent reactions with a pH optimum of 7.9. Transglutaminase activity was shown to increase over a 2-week growth period in both the roots and leaves of pea. The product of transglutaminase's protein-cross-linking activity, ε-(γ-glutamyl)-lysine isodipeptide, was detected in root and shoot protein from pea, broad bean, wheat, and barley by cation-exchange chromatography. The presence of the isodipeptide was confirmed by reversed-phase chromatography. Hydrolysis of the isodipeptide after cation-exchange chromatography confirmed the presence of glutamate and lysine.

Documentos Relacionados

• Plasticity and adaptation of Ca2+ signaling and Ca2+-dependent exocytosis in SERCA2+/– mice
• Ca2+-binding activity of a COOH-terminal fragment of the Drosophila BK channel involved in Ca2+-dependent activation
• Relocation of a Ca2+-dependent protein kinase activity during pollen tube reorientation
• Mechanism of Ca2+-dependent nuclear accumulation of calmodulin
• Stowaway: a new family of inverted repeat elements associated with the genes of both monocotyledonous and dicotyledonous plants.