Resolution of Ca2+—calmodulin‐activated protein kinase from wheat germ
- 13 December 1982
- journal article
- Published by Wiley in FEBS Letters
- Vol. 150 (1) , 167-171
- https://doi.org/10.1016/0014-5793(82)81327-6
Abstract
A soluble Ca2+‐ and Ca2+—calmodulin‐activated protein kinase was partially purified from wheat germ. The phosphorylation of histones and casein catalyzed by this enzyme is largely Ca2+‐dependent. After repeated gel filtration of the protein kinase in the presence of 1 mM EGTA, the phosphorylation of casein and histones by the enzyme is activated 3‐fold and up to 16‐fold, respectively, by added calmodulin (12.5 μM). Such activation of the protein kinase by calmodulin is Ca2+‐dependent. The protein kinase binds to calmodulin—Sepharose 4B in a Ca2+‐dependent fashion. This type of Ca2+‐activated protein kinase may be involved in stimulus—response coupling in plants.Keywords
This publication has 15 references indexed in Scilit:
- Free Ca2+ and cytoplasmic streaming in the alga CharaNature, 1982
- The role of protein phosphorylation in neural and hormonal control of cellular activityNature, 1982
- Resolution and Properties of Two High Affinity Cyclic Adenosine 3′:5′-monophosphate-Binding Proteins from Wheat GermPlant Physiology, 1981
- A calmodulin‐dependent, microsomal ATPase from corn (Zea mays L.)FEBS Letters, 1981
- Spinach calmodulin: isolation, characterization, and comparison with vertebrate calmodulinsBiochemistry, 1980
- Calmodulin activation of plant microsomal Ca 2+ uptakeProceedings of the National Academy of Sciences, 1980
- Characterization of the plant nicotinamide adenine dinucleotide kinase activator protein and its identification as calmodulinBiochemistry, 1980
- Calcium-dependent regulator of NAD kinase in higher plantsBiochemical and Biophysical Research Communications, 1978
- 2,4-Dichlorophenoxyacetic Acid-enhanced Phosphorylation of Soybean Nuclear ProteinsPlant Physiology, 1978
- Regulation of the Phosphorylation of Chromatin-associated Proteins in Lemna and HordeumPlant Physiology, 1975