Although a well ascertained evidence proves that the activity of the plant plasma membrane H+-ATPase is regulated by 14-3-3 proteins, information about physiological factors modulating the phosphorylation-dependent association between 14-3-3 proteins and the proton pump is largely incomplete. In this paper we show that the 5 ' -AMP-mimetic, 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR), inhibits the fusicoccin-promoted proton extrusion in maize roots. We also demonstrate that 5 ' -AMP inhibits the association of 14-3-3 proteins with the C-terminal domain of the H+-ATPase in an overlay assay as well as the 14-3-3-dependent stimulation of the Arabidopsis thaliana H+-ATPase AHA1 isoform expressed in yeast membranes. Finally, by means of affinity chromatography with immobilized 5 ' -AMP and trinitrophenyl-AMP fluorescence analysis, we demonstrate that the 14-3-3 isoform GF14-6 from maize is able to bind 5 ' -AMP. The possible role of 5 ' -AMP as a general regulator of 14-3-3 functions in the plant cell is discussed.

Camoni, L., Visconti, S., Marra, M., & Aducci, P. (2001). Adenosine 5 '-monophosphate inhibits the association of 14-3-3 proteins with the plant plasma membrane H+-ATPase. THE JOURNAL OF BIOLOGICAL CHEMISTRY, 276(34), 31709-31712.

Adenosine 5 '-monophosphate inhibits the association of 14-3-3 proteins with the plant plasma membrane H+-ATPase

CAMONI, LORENZO;VISCONTI, SABINA;MARRA, MAURO;ADUCCI, PATRIZIA
2001

Abstract

Although a well ascertained evidence proves that the activity of the plant plasma membrane H+-ATPase is regulated by 14-3-3 proteins, information about physiological factors modulating the phosphorylation-dependent association between 14-3-3 proteins and the proton pump is largely incomplete. In this paper we show that the 5 ' -AMP-mimetic, 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR), inhibits the fusicoccin-promoted proton extrusion in maize roots. We also demonstrate that 5 ' -AMP inhibits the association of 14-3-3 proteins with the C-terminal domain of the H+-ATPase in an overlay assay as well as the 14-3-3-dependent stimulation of the Arabidopsis thaliana H+-ATPase AHA1 isoform expressed in yeast membranes. Finally, by means of affinity chromatography with immobilized 5 ' -AMP and trinitrophenyl-AMP fluorescence analysis, we demonstrate that the 14-3-3 isoform GF14-6 from maize is able to bind 5 ' -AMP. The possible role of 5 ' -AMP as a general regulator of 14-3-3 functions in the plant cell is discussed.
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/04
English
Con Impact Factor ISI
Adenosinetriphosphate; Bioassay; Biological membranes; Hydrogen; Physiology; Plants (botany); Plasmas; Protons; Plasma membranes; Biochemistry; 5 amino 4 imidazolecarboxamide riboside; adenosine phosphate; fusicoccin; protein 14 3 3; proton pump; proton transporting adenosine triphosphatase; trinitrophenyl; vegetable protein; tyrosine 3 monooxygenase; affinity chromatography; Arabidopsis; article; carboxy terminal sequence; cell membrane; fluorescence spectroscopy; maize; nonhuman; phosphorylation; plant; polyacrylamide gel electrophoresis; priority journal; protein protein interaction; Saccharomyces cerevisiae; amino acid sequence; drug antagonism; enzymology; metabolism; molecular genetics; spectrofluorometry; Arabidopsis; Arabidopsis thaliana; Saccharomyces; Saccharomyces cerevisiae; Zea mays; 14-3-3 Proteins; Adenosine Monophosphate; Amino Acid Sequence; Arabidopsis; Cell Membrane; Molecular Sequence Data; Proton-Translocating ATPases; Spectrometry, Fluorescence; Tyrosine 3-Monooxygenase; Zea mays
Camoni, L., Visconti, S., Marra, M., & Aducci, P. (2001). Adenosine 5 '-monophosphate inhibits the association of 14-3-3 proteins with the plant plasma membrane H+-ATPase. THE JOURNAL OF BIOLOGICAL CHEMISTRY, 276(34), 31709-31712.
Camoni, L; Visconti, S; Marra, M; Aducci, P
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2108/41250
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