PMID: 9535278Apr 16, 1998Paper

High-pressure effects on vacuolar H+-ATPase from etiolated mung bean seedlings

Journal of Protein Chemistry
Y R TsaiR L Pan

Abstract

A high-hydrostatic-pressure technique was employed to study the structure-function relationship of plant vacuolar H+-ATPase from etiolated mung bean seedlings (Vigna radiata L.). When isolated vacuolar H+-ATPase was subjected to hydrostatic pressure, the activity of ATP hydrolysis was markedly inhibited in a time-, protein concentration- and pressure-dependent manner. The pressure treatment decreased both Vmax and Km of solubilized vacuolar H+-ATPase, implying an increase in ATP binding affinity, but a decrease in the ATP hydrolysis activity. Physiological substrate, Mg2+-ATP, augmented the loss of enzymatic activity upon pressure treatment. However, ADP, AMP, and Pi exerted substantial protective effects against pressurization. Steady-state ATP hydrolysis was more sensitive to pressurization than single-site ATPase activity. The inactivation of solubilized vacuolar H+-ATPase by pressure may result from changes in protein-protein interaction. The conformational change of solubilized vacuolar H+-ATPase induced by hydrostatic pressure was further determined by spectroscopic techniques. The inhibition of vacuolar H+-ATPase under pressurization involved at least two steps. Taken together, our work indicates that subunit-subunit int...Continue Reading

Citations

Mar 1, 2006·Functional Plant Biology : FPB·Fan S ChiuRong L Pan
Jun 22, 2001·Biochimica Et Biophysica Acta·C L ChuR L Pan
Aug 26, 1999·International Journal of Pharmaceutics·W Wang

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