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Updated: Oct 16, 2026

Affinity Purification of Chloroplast Translocon Protein Complexes Using the TAP Tag
Published on: November 1, 2018
Identification, purification, and molecular cloning of a putative plastidic glucose translocator
A Weber1, J C Servaites, D R Geiger
1Universität zu Köln, Lehrstuhl Botanik II, Gyrhofstrasse 15, D-50931 Cologne, Germany. andr.weber@uni-koeln.de
Abstract:
During photosynthesis, part of the fixed carbon is directed into the synthesis of transitory starch, which serves as an intermediate carbon storage facility in chloroplasts. This transitory starch is mobilized during the night. Increasing evidence indicates that the main route of starch breakdown proceeds by way of hydrolytic enzymes and results in glucose formation. This pathway requires a glucose translocator to mediate the export of glucose from the chloroplasts. We have reexamined the kinetic properties of the plastidic glucose translocator and, using a differential labeling procedure, have identified the glucose translocator as a component of the inner envelope membrane. Peptide sequence information derived from this protein was used to isolate cDNA clones encoding a putative plastidic glucose translocator from spinach, potato, tobacco, Arabidopsis, and maize. We also present the molecular characterization of a candidate for a hexose transporter of the plastid envelope membrane. This transporter, initially characterized more than 20 years ago, is closely related to the mammalian glucose transporter GLUT family and differs from all other plant hexose transporters that have been characterized to date.
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