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THE PLANT CELL, Vol 7, Issue 12 2053-2067, Copyright © 1995 by American Society of Plant Biologists
Immunocytological Localization of an Epitope-Tagged Plasma Membrane Proton Pump (H+-ATPase) in Phloem Companion Cells
N. D. DeWitt and M. R. Sussman
Cell and Molecular Biology Program and Department of Horticulture, University of Wisconsin, 1575 Linden Drive, Madison, Wisconsin 53706-1590
In higher plants, the plasma membrane proton pump (H+-ATPase) is encoded by
a surprisingly large multigene family whose members are expressed in
different tissues. Using an 18-amino acid epitope tag derived from the
animal oncogene c-Myc, we have performed immunocytolocalization
measurements of the protein expressed by one member of this family, AHA3
(Arabidopsis H+-ATPase isoform 3). Immunofluorescence studies with tissue
sections of transgenic plants have revealed that c-Myc-tagged AHA3 is
restricted to the plasma membrane of phloem companion cells, whereas other
AHA isoproteins are more widely distributed in the plasma membrane of other
cell types. Electron microscopy with immunogold-labeled tissue sections
suggests that there is a high concentration of proton pumps in the plasma
membrane of companion cells but a much lower concentration in the plasma
membrane of sieve elements. Due to plasmodesmata connecting the plasma
membrane of these two adjacent cell types, it is likely that the proton
motive force generated by the proton pump in companion cells can serve to
power the uptake of sugar by proton-coupled symporters in either the
companion cell or sieve element cell. The abundance of the proton pump in
the plasma membrane of companion cells supports an apoplastic model for
phloem loading in which the metabolic energy that drives sugar uptake is
consumed by AHA3 at the companion cell plasma membrane. These experiments
with a genetically altered integral plasma membrane protein demonstrate the
utility of using a short c-Myc sequence as an epitope tag in Arabidopsis.
Furthermore, our results demonstrate that, using genes encoding individual
members of a gene family, it is possible to label plasma membrane proteins
immunologically in specific, differentiated cell types of higher plants.
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