DURING photosynthetic CO2 fixation, fixed carbon is exported from the chloroplasts in the form of triose phosphate by the chloroplast phosphate translocator, which is the principal polypeptide (E29) from spinach chloroplast envelopes1. We have sequenced this nuclear-coded envelope membrane protein from both spinach and pea chloroplasts2,3. An envelope membrane protein, E30, has been identified as a possible receptor for protein import into pea chloroplasts using an anti-idiotypic antibody approach4–6; antibodies raised against purified E30 inhibited binding and import of proteins into chloroplasts7. The amino-acid sequence of E30 deduced from its complementary DNA7 turned out to be highly homologous to that of E29, assigned by us as the spinach phosphate translocator2, and was identical to the corresponding polypeptide from pea chloroplasts3. Differences in the binding properties to hydroxylapatite of £30 and the phosphate translocator suggested that E30 was not responsible for the chloroplast phosphate-transport activity but was the chloroplast import receptor7. Here we present evidence that argues against this and which identifies E30 as the chloroplast phosphate translocator.
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Flügge, UI., Weber, A., Fischer, K. et al. The major chloroplast envelope polypeptide is the phosphate translocator and not the protein import receptor. Nature 353, 364–367 (1991). https://doi.org/10.1038/353364a0
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