Regulation of the activity of N-1-naphthylphthalamic acid binding protein by ATP and phosphatase
N-1-naphthylphthalamic acid (NPA), an auxin transport inhibitor, was found to bind specifically to a crude membrane preparation from sugar beet seedling leaf cell suspension cultures. The dissociation constant (Kd) and binding protein concentration were found to be 1.71 μmol dm -3 and 220 pmol g -1(membrane protein), respectively. The amount of specific 3H-NPA binding was significantly increased by adding Mg 2+ATP to the binding assay solution. Treatment of membrane preparations with acid phosphatase, prior to the NPA binding assay, resulted in lower specific binding. ATP activation and phosphatase inactivation were culture stage dependent. Although a considerable effect could be detected when using cells from day 8 (representing the linear phase), the same treatment did not alter the binding if cells from day 1 (representing lag phase) or day 14 (representing the stationary phase) were used. These observations have strongly highlighted the possible involvement of a phosphorylation and dephosphorylation mechanism in vivo in the regulation of the activity of the NPA binding protein. High phosphatase activity was found in the supernatant, but not in the membrane pellet) after 50 000 g centrifugation. Our present study has indicated that receptor activity could be regulated by a phosphorylation and dephosphorylation mechanism in plants.
|Keywords||auxin transport, Beta vulgaris, receptor phosphorylation|
Zhang, Y.-H. (Y. H.), Xing, T, Hall, J.F. (J. F.), Barker, R.D.J. (R. D J), & Elliott, M.C. (M. C.). (2004). Regulation of the activity of N-1-naphthylphthalamic acid binding protein by ATP and phosphatase. Biologia Plantarum, 47(4), 493–499. doi:10.1023/B:BIOP.0000041052.31348.a0