NDLI: Purification of a nitrate reductase kinase from Spinacea oleracea leaves, and its identification as a calmodulin-domain protein kinase

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Purification of a nitrate reductase kinase from Spinacea oleracea leaves, and its identification as a calmodulin-domain protein kinase

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Planta : Volume 206, Issue 1, July 1998

Purification of a nitrate reductase kinase from Spinacea oleracea leaves, and its identification as a calmodulin-domain protein kinase

Content Provider	Springer Nature Link
Author	Douglas, Pauline Moorhead, Greg Hong, Yan Morrice, Nick MacKintosh, Carol
Copyright Year	1998
Abstract	Spinach (Spinacea oleracea L.) nitrate reductase (NR) is inactivated by phosphorylation on serine-543, followed by binding of the phosphorylated enzyme to 14-3-3 proteins. We purified one of several chromatographically distinct NRserine-543 kinases from spinach leaf extracts, and established by Edman sequencing of 80 amino acid residues that it is a calcium-dependent (calmodulin-domain) protein kinase (CDPK), with peptide sequences very similar to Arabidopsis CDPK6 (accession no. U20623; also known as CPK3). The spinach CDPK was recognized by antibodies raised against Arabidopsis CDPK. Nitrate reductase was phosphorylated at serine-543 by bacterially expressed His-tagged CDPK6, and the phosphorylated NR was inhibited by 14-3-3 proteins. However, the bacterially expressed CDPK6 had a specific activity approx. 200-fold lower than that of the purified spinach enzyme. The physiological control of NR by CDPK is discussed, and the regulatory properties of the purified CDPK are considered with reference to current models for reversible intramolecular binding of the calmodulin-like domain to the autoinhibitory junction of CDPKs.
Starting Page	435
Ending Page	442
Page Count	8
File Format	PDF
ISSN	00320935
Journal	Planta
Volume Number	206
Issue Number	3
e-ISSN	14322048
Language	English
Publisher	Springer-Verlag
Publisher Date	1998-08-24
Publisher Place	Berlin/Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Content Type	Text
Resource Type	Article
Subject	Genetics Plant Science

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Identification of a Protein That Inhibits the Phosphorylated Form of Nitrate Reductase from Spinach (Spinacia oleracea) Leaves.

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Identity of an ABA-activated 46 kDa mitogen-activated protein kinase from Zea mays leaves: partial purification, identification and characterization

Nitrate reductases from leaves of Ricinus (Ricinus communis L.) and spinach (Spinacia oleracea L.) have different regulatory properties

The activation state of nitrate reductase is not always correlated with total nitrate reductase activity in leaves

Properties of nitrate reductase from seedling leaves of selected barley genotypes

Boron deficiency causes a drastic decrease in nitrate content and nitrate reductase activity, and increases the content of carbohydrates in leaves from tobacco plants

Fluctuations in Spinach Leaf Nitrate Reductase During Light-Dark Transitions

Purification of a nitrate reductase kinase from Spinacea oleracea leaves, and its identification as a calmodulin-domain protein kinase

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