A protein kinase activity associated with maize root plasma membranes was partially purified and characterized. Biochemical properties, such as calcium dependence, inhibition by calmodulin antagonists, and absence of calmodulin stimulation; indicated that the enzyme belongs to the calcium-dependent protein kinase (CDPK) family. By means of an in-gel phosphorylation assay the molecular mass of active polypeptides was determined: two bands of 55 and 51 kDa became labelled. The same proteins were also immunodecorated by monoclonal antibodies against soybean CDPK. Results from in vitro assays demonstrated that maize H+-ATPase was a suitable substrate for this protein kinase and that the phosphorylation site was located at the C-terminal domain of the enzyme. This result was confirmed by using as substrate in phosphorylation assays the isolated C-terminal domain of the H+- ATPase expressed in Escherichia coli as a glutathione-transferase fusion protein.

Camoni, L., Fullone, M., Marra, M., Aducci, P. (1998). The plasma membrane H+-ATPase from maize roots is phosphorylated in the C-terminal domain by a calcium-dependent protein kinase. PHYSIOLOGIA PLANTARUM, 104(4), 549-555 [10.1034/j.1399-3054.1998.1040405.x].

The plasma membrane H+-ATPase from maize roots is phosphorylated in the C-terminal domain by a calcium-dependent protein kinase

CAMONI, LORENZO;MARRA, MAURO;ADUCCI, PATRIZIA
1998-01-01

Abstract

A protein kinase activity associated with maize root plasma membranes was partially purified and characterized. Biochemical properties, such as calcium dependence, inhibition by calmodulin antagonists, and absence of calmodulin stimulation; indicated that the enzyme belongs to the calcium-dependent protein kinase (CDPK) family. By means of an in-gel phosphorylation assay the molecular mass of active polypeptides was determined: two bands of 55 and 51 kDa became labelled. The same proteins were also immunodecorated by monoclonal antibodies against soybean CDPK. Results from in vitro assays demonstrated that maize H+-ATPase was a suitable substrate for this protein kinase and that the phosphorylation site was located at the C-terminal domain of the enzyme. This result was confirmed by using as substrate in phosphorylation assays the isolated C-terminal domain of the H+- ATPase expressed in Escherichia coli as a glutathione-transferase fusion protein.
1998
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/04 - FISIOLOGIA VEGETALE
English
Con Impact Factor ISI
CALMODULIN-LIKE DOMAIN; PLANT DEFENSE RESPONSE; FUNGAL PATHOGENS; SENSITIVE METHOD; FUSICOCCIN; PURIFICATION; ACTIVATION; BINDING; CDPK
7
Camoni, L., Fullone, M., Marra, M., Aducci, P. (1998). The plasma membrane H+-ATPase from maize roots is phosphorylated in the C-terminal domain by a calcium-dependent protein kinase. PHYSIOLOGIA PLANTARUM, 104(4), 549-555 [10.1034/j.1399-3054.1998.1040405.x].
Camoni, L; Fullone, M; Marra, M; Aducci, P
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/41254
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