Malik MK, Reddy AS, Wang ZQ, Czernik AJ, Poovaiah BW.
ASGSB Bull. 1993 Oct; 7: 68.
Dept. of Horticulture, Washington State Univ., Pullman 99164.
The presence of Ca2+/calmodulin-dependent protein kinase in corn root tips was investigated using affinity purified antipeptide antibodies produced against alpha subunit of rat brain Ca2+/calmodulin-dependent protein kinase (CaM KII). Three different antibodies raised against CaM KII recognized a 56 kDa protein in soluble protein fraction isolated from corn root tips. The molecular weight of the crossreacting plant protein is similar to the mammalian CaM KII. After immunoprecipitating the 56 kDa protein, kinase activity was assayed using gel phosphorylation method. The results revealed that the immunoprecipitated protein has Ca2+/calmodulin-dependent autophosphorylation activity, a characteristic of mammalian multifunctional CaM KII. CaM KII inhibitors such as KN-62 and a peptide (corresponding to amino acids 281-309 of alpha subunit of CaM KII) inhibited phosphorylation of the 56 kDa protein in vitro. Soluble extract from corn roots phosphorylated synapsin I, a physiological substrate for mammalian Ca2+/calmodulin-dependent protein kinases and this phosphorylation of synapsin I was stimulated by Ca2+ and calmodulin. Phosphopeptide mapping revealed that the site of enhanced phosphorylation of synapsin I was located within the 30 kDa fragment that is the known site of phosphorylation by CaM KII. These results indicate that plants contain a Ca2+/calmodulin-dependent protein kinase with properties similar to mammalian CaM KII.
Publication Types:
Keywords:
- 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine
- Animals
- Calcium
- Calcium Channels
- Calcium-Calmodulin-Dependent Protein Kinase Type 2
- Calcium-Calmodulin-Dependent Protein Kinases
- Calmodulin
- Calmodulin-Binding Proteins
- In Vitro
- KN 62
- Phosphorylation
- Rats
- Synapsins
- NASA Discipline Number 40-50
- NASA Discipline Plant Biology
- NASA Program Space Biology
- Non-NASA Center
Other ID:
UI: 102212864
From Meeting Abstracts