Cloning and in vivo expression of functional triose phosphate/phosphate translocators from C3- and C4-plants: evidence for the putative participation of specific amino acid residues in the recognition of phosphoenolpyruvate.

@article{Fischer1994CloningAI,
  title={Cloning and in vivo expression of functional triose phosphate/phosphate translocators from C3- and C4-plants: evidence for the putative participation of specific amino acid residues in the recognition of phosphoenolpyruvate.},
  author={Klaus D. Fischer and Bettina Arbinger and Beno{\^i}t Kammerer and Christian Busch and Susanne Brink and H. Wallmeier and Norbert Sauer and Christoph Eckerskorn and Ulf Ingo Fl{\"u}gge},
  journal={The Plant journal : for cell and molecular biology},
  year={1994},
  volume={5 2},
  pages={215-26}
}
The primary sequences of the chloroplast triose phosphate/phosphate translocator precursor proteins from C4-plants (maize mesophyll cells and Flaveria trinervia) and from the C3-type Flaveria pringlei were determined. The mature parts of these translocators possess 83-94% identical amino acid residues. The C4-translocator protein can be correctly targeted to C3-type chloroplasts and inserted into the envelope membrane. Expression of the mature parts of these chloroplast translocators (cTPT) in… CONTINUE READING

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