Proteolytic activation of the plant plasma membrane H+-ATPase by removal of a terminal segment
Research output: Contribution to journal › Journal article › Research › peer-review
Incubation of oat root plasma membrane vesicles in the presence of ATP with trypsin or chymotrypsin increased the rate of ATP hydrolysis and ATP-dependent proton pumping by the plasma membrane H+-ATPase. Proton pumping was stimulated more than 200%, whereas ATP hydrolytic activity was stimulated about 30%. The K(m)(ATP) for both proton pumping and ATP hydrolysis was lowered from about 0.3 mM to below 0.1 mM. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of trypsin-treated plasma membranes revealed a decrease in a 100-kDa band and the appearance of a 93-kDa band. Western blot analysis using antibodies against the H+-ATPase showed that both of these bands represented the H+-ATPase and suggested that a 7-kDa segment was released. Extensive treatment with cardoxypeptidase A also activated the H+-ATPase indicating that the 7-kDa segment originated from the C terminus.
Original language | English |
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Journal | Journal of Biological Chemistry |
Volume | 265 |
Issue number | 23 |
Pages (from-to) | 13423-13426 |
Number of pages | 4 |
ISSN | 0021-9258 |
Publication status | Published - 1990 |
ID: 245001434