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Activation of the Dunaliella acidophila Plasma Membrane H+-ATPase by Trypsin Cleavage of a Fragment That Contains a Phosphorylation Site

I. Sekler, M. Weiss, U. Pick
I. Sekler
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M. Weiss
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U. Pick
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Published August 1994. DOI: https://doi.org/10.1104/pp.105.4.1125

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Abstract

Trypsin treatment of purified H+-ATPase from plasma membranes of the extreme acidophilic alga Dunaliella acidophila enhances ATP hydrolysis and H+ pumping activities. The activation is associated with an alkaline pH shift, an increase in Vmax, and a decrease in Km(ATP). The activation is correlated with cleavage of the 100-kD ATPase polypeptide to a fragment of approximately 85 kD and the appearance of three minor hydrophobic fragments of 7 to 8 kD, which remain associated with the major 85-kD polypeptide. The N-terminal sequence of the small fragments has partial homology to residues 713 to 741 of Arabidopsis thaliana plasma membrane H+-ATPases. Incubation of cells with 32P-labeled orthophosphate (32Pi) results in incorporation of 32P into the ATPase 100-kD polypeptide. Trypsin treatment of the 32Pi-labeled ATPase leads to complete elimination of label from the approximately 85-kD polypeptide. Cleavage of the phosphorylated enzyme with endoproteinase Glu-C (V-8) yields a phosphorylated 12-kD fragment. Peptide mapping comparison between the 100-kD and the trypsinized 85-kD polypeptides shows that the 12-kD fragment is derived from the trypsin-cleaved part of the enzyme. The N-terminal sequence of the 12-kD fragment closely resembles a C-terminal stretch of an ATPase from another Dunaliella species. It is suggested that trypsin activation of the D. acidophila plasma membrane H+-ATPase results from elimination of an autoinhibitory domain at the C-terminal end of the enzyme that carries a vicinal phosphorylation site.

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Activation of the Dunaliella acidophila Plasma Membrane H+-ATPase by Trypsin Cleavage of a Fragment That Contains a Phosphorylation Site
I. Sekler, M. Weiss, U. Pick
Plant Physiology Aug 1994, 105 (4) 1125-1132; DOI: 10.1104/pp.105.4.1125

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Activation of the Dunaliella acidophila Plasma Membrane H+-ATPase by Trypsin Cleavage of a Fragment That Contains a Phosphorylation Site
I. Sekler, M. Weiss, U. Pick
Plant Physiology Aug 1994, 105 (4) 1125-1132; DOI: 10.1104/pp.105.4.1125
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Plant Physiology
Vol. 105, Issue 4
Aug 1994
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  • Characterization of a Red Beet Protein Homologous to the Essential 36-Kilodalton Subunit of the Yeast V-Type ATPase
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