fusicoccin and oxophenylarsine

fusicoccin has been researched along with oxophenylarsine* in 2 studies

Other Studies

2 other study(ies) available for fusicoccin and oxophenylarsine

Article	Year
14-3-3 protein-activated and autoinhibited forms of plasma membrane H(+)-ATPase. Biochemical and biophysical research communications, 2001, Sep-07, Volume: 286, Issue:5 Several authors previously showed that the interaction between 14-3-3 proteins and plasma membrane H(+)-ATPase leads to an activated complex in which the enzyme is endowed with more favorable kinetic parameters and a more physiological pH optimum. In this paper we report immunological studies with antibodies covering a different specific region of the protein, including the N- and the C-terminal ends. The results showed that, beside a free and a complexed form, a third form of H(+)-ATPase in the cell must exist with low activity and no more activation due to the loss of a part of the C-terminal regulatory domain. A model in which 14-3-3 proteins activate H(+)-ATPase by protecting it from a specific proteolytic attack is presented and its generalization is discussed. Topics: 14-3-3 Proteins; Amino Acid Sequence; Arsenicals; Blotting, Western; Cell Membrane; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Enzyme Inhibitors; Ethylmaleimide; Glycosides; Glycosylation; Hydrogen-Ion Concentration; Immunoblotting; Models, Biological; Molecular Sequence Data; Phosphorylation; Phosphothreonine; Phosphotyrosine; Plant Proteins; Precipitin Tests; Protein Binding; Protein Structure, Tertiary; Proton-Translocating ATPases; Sequence Homology, Amino Acid; Tyrosine 3-Monooxygenase	2001
Phenylarsine oxide inhibits the fusicoccin-induced activation of plasma membrane H(+)-ATPase. Plant physiology, 2000, Volume: 122, Issue:2 To investigate the mechanism by which fusicoccin (FC) induces the activation of the plasma membrane (PM) H(+)-ATPase, we used phenylarsine oxide (PAO), a known inhibitor of protein tyrosine-phosphatases. PAO was supplied in vivo in the absence or presence of FC to radish (Raphanus sativus L.) seedlings and cultured Arabidopsis cells prior to PM extraction. Treatment with PAO alone caused a slight decrease of PM H(+)-ATPase activity and, in radish, a decrease of PM-associated 14-3-3 proteins. When supplied prior to FC, PAO drastically inhibited FC-induced activation of PM H(+)-ATPase, FC binding to the PM, and the FC-induced increase of the amount of 14-3-3 associated with the PM. On the contrary, PAO was completely ineffective on all of the above-mentioned parameters when supplied after FC. The H(+)-ATPase isolated from PAO-treated Arabidopsis cells maintained the ability to respond to FC if supplied with exogenous, nonphosphorylated 14-3-3 proteins. Altogether, these results are consistent with a model in which the dephosphorylated state of tyrosine residues of a protein(s), such as 14-3-3 protein, is required to permit FC-induced association between the 14-3-3 protein and the PM H(+)-ATPase. Topics: Arsenicals; Brassica; Cell Membrane; Enzyme Activation; Glycosides; Proton-Translocating ATPases	2000

Article

Year

14-3-3 protein-activated and autoinhibited forms of plasma membrane H(+)-ATPase.

Biochemical and biophysical research communications, 2001, Sep-07, Volume: 286, Issue:5

Several authors previously showed that the interaction between 14-3-3 proteins and plasma membrane H(+)-ATPase leads to an activated complex in which the enzyme is endowed with more favorable kinetic parameters and a more physiological pH optimum. In this paper we report immunological studies with antibodies covering a different specific region of the protein, including the N- and the C-terminal ends. The results showed that, beside a free and a complexed form, a third form of H(+)-ATPase in the cell must exist with low activity and no more activation due to the loss of a part of the C-terminal regulatory domain. A model in which 14-3-3 proteins activate H(+)-ATPase by protecting it from a specific proteolytic attack is presented and its generalization is discussed.

Topics: 14-3-3 Proteins; Amino Acid Sequence; Arsenicals; Blotting, Western; Cell Membrane; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Enzyme Inhibitors; Ethylmaleimide; Glycosides; Glycosylation; Hydrogen-Ion Concentration; Immunoblotting; Models, Biological; Molecular Sequence Data; Phosphorylation; Phosphothreonine; Phosphotyrosine; Plant Proteins; Precipitin Tests; Protein Binding; Protein Structure, Tertiary; Proton-Translocating ATPases; Sequence Homology, Amino Acid; Tyrosine 3-Monooxygenase

2001

Phenylarsine oxide inhibits the fusicoccin-induced activation of plasma membrane H(+)-ATPase.

Plant physiology, 2000, Volume: 122, Issue:2

To investigate the mechanism by which fusicoccin (FC) induces the activation of the plasma membrane (PM) H(+)-ATPase, we used phenylarsine oxide (PAO), a known inhibitor of protein tyrosine-phosphatases. PAO was supplied in vivo in the absence or presence of FC to radish (Raphanus sativus L.) seedlings and cultured Arabidopsis cells prior to PM extraction. Treatment with PAO alone caused a slight decrease of PM H(+)-ATPase activity and, in radish, a decrease of PM-associated 14-3-3 proteins. When supplied prior to FC, PAO drastically inhibited FC-induced activation of PM H(+)-ATPase, FC binding to the PM, and the FC-induced increase of the amount of 14-3-3 associated with the PM. On the contrary, PAO was completely ineffective on all of the above-mentioned parameters when supplied after FC. The H(+)-ATPase isolated from PAO-treated Arabidopsis cells maintained the ability to respond to FC if supplied with exogenous, nonphosphorylated 14-3-3 proteins. Altogether, these results are consistent with a model in which the dephosphorylated state of tyrosine residues of a protein(s), such as 14-3-3 protein, is required to permit FC-induced association between the 14-3-3 protein and the PM H(+)-ATPase.

Topics: Arsenicals; Brassica; Cell Membrane; Enzyme Activation; Glycosides; Proton-Translocating ATPases

2000