Plant Calreticulin Is Specifically and Efficiently Phosphorylated by Protein Kinase CK2

Plant Calreticulin Is Specifically and Efficiently Phosphorylated by Protein Kinase CK2 Calreticulin isolated from spinach leaves has been specifically phosphorylated in vitro by protein kinase CK2 while animal calreticulin from rabbit liver is not a substrate of this kinase under the same conditions. Phosphoserine is the only phosphoamino acid detected. High affinity binding (Km=4.4 μM) and a nearly stoichiometric incorporation of phosphate was determined. Partially purified spinach calreticulin is phosphorylated at the same site(s) by a copurifying protein kinase sharing biochemical properties very similar if not identical to those of mammalian CK2. Other plant calreticulins isolated from Liriodendron tulipifera appear to be also phosphorylated by CK2. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biochemical and Biophysical Research Communications Elsevier

Plant Calreticulin Is Specifically and Efficiently Phosphorylated by Protein Kinase CK2

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Publisher
Elsevier
Copyright
Copyright © 1996 Academic Press
ISSN
0006-291x
D.O.I.
10.1006/bbrc.1996.0625
Publisher site
See Article on Publisher Site

Abstract

Calreticulin isolated from spinach leaves has been specifically phosphorylated in vitro by protein kinase CK2 while animal calreticulin from rabbit liver is not a substrate of this kinase under the same conditions. Phosphoserine is the only phosphoamino acid detected. High affinity binding (Km=4.4 μM) and a nearly stoichiometric incorporation of phosphate was determined. Partially purified spinach calreticulin is phosphorylated at the same site(s) by a copurifying protein kinase sharing biochemical properties very similar if not identical to those of mammalian CK2. Other plant calreticulins isolated from Liriodendron tulipifera appear to be also phosphorylated by CK2.

Journal

Biochemical and Biophysical Research CommunicationsElsevier

Published: Apr 25, 1996

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