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THE PLANT CELL, Vol 9, Issue 3 453-462, Copyright © 1997 by American Society of Plant Biologists
A New Class of Plastidic Phosphate Translocators: A Putative Link between Primary and Secondary Metabolism by the Phosphoenolpyruvate/Phosphate Antiporter
K. Fischer, B. Kammerer, M. Gutensohn, B. Arbinger, A. Weber, R. E. Hausler and U. I. Flugge
Botanisches Institut der Universitat zu Koln, Lehrstuhl II, Gyrhofstrasse 15, D-50931 Cologne, Germany
We have purified a plastidic phosphate transport protein from maize
endosperm membranes and cloned and sequenced the corresponding cDNAs from
maize endosperm, maize roots, cauliflower buds, tobacco leaves, and
Arabidopsis leaves. All of these cDNAs exhibit high homology to each other
but only ~30% identity to the known chloroplast triose phosphate/phosphate
translocators. The corresponding genes are expressed in both
photosynthetically active tissues and in nongreen tissues, although
transcripts were more abundant in nongreen tissues. Expression of the
coding region in transformed yeast cells and subsequent transport
measurements of the purified recombinant translocator showed that the
protein mediates transport of inorganic phosphate in exchange with C3
compounds phosphorylated at C-atom 2, particularly phosphoenolpyruvate,
which is required inside the plastids for the synthesis of, for example,
aromatic amino acids. This plastidic phosphate transporter is thus
different in structure and function from the known triose
phosphate/phosphate translocator. We propose that plastids contain various
phosphate translocators with overlapping substrate specificities to ensure
an efficient supply of plastids with a single substrate, even in the
presence of other phosphorylated metabolites.
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