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PLANT PHYSIOLOGY , Vol 111, Issue 2 427-432, Copyright © 1996 by American Society of Plant Biologists
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DEVELOPMENT AND GROWTH REGULATION |
The N-1-Naphthylphthalamic Acid-Binding Protein Is an Integral Membrane Protein
P. Bernasconi, B. C. Patel, J. D. Reagan and M. V. Subramanian
Sandoz Agro Inc., Research Division, 975 California Avenue, Palo Alto, California 94304-1104
N-1-Naphthylphthalmic acid (NPA)-binding protein is a plasmalemma (PM)
protein involved in the control of cellular auxin efflux. We re-evaluated
the spatial relationship of this protein with the PM of zucchini (Cucurbita
pepo L.) hypocotyls. First, Triton X-114 partitioning indicated that the
NPA-binding protein was more hydrophobic than most PM proteins. Second, the
NPA-binding activity was found to be resistant to proteolytic digestion in
membranes. Maximum concentrations of binding sites for NPA were virtually
identical in untreated and proteinase K-treated PMs: 19.2 and 20.6 pmol
[3H]NPA bound/mg protein, respectively. The insensitivity of the
NPA-binding protein was not due to its presence inside tightly sealed
vesicles or due to lack of protease activity in the conditions tested. This
protein could be made sensitive to proteolytic degradation upon
solubilization by 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate
in the presence of sodium molybdate. Proteinase K treatment decreased the
concentration of binding sites to 0.84 pmol [3H]NPA bound/mg protein from
9.2 for untreated, solubilized PM. Third, this activity could not be
solubilized by chaotropic agents or sodium carbonate treatment of intact
PM. This study indicates that the NPA-binding protein may be an integral
membrane protein and contradicts previously reported findings that
suggested that this protein was peripheral to the PM.
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