Characterization of Tic110, a channel-forming protein at the inner envelope membrane of chloroplasts, unveils a response to Ca(2+) and a stromal regulatory disulfide bridge.

@article{Balsera2009CharacterizationOT,
  title={Characterization of Tic110, a channel-forming protein at the inner envelope membrane of chloroplasts, unveils a response to Ca(2+) and a stromal regulatory disulfide bridge.},
  author={M{\'o}nica Balsera and Tom Alexander Goetze and Erika Kov{\'a}cs-Bogd{\'a}n and Peter Sch{\"u}rmann and Richard Wagner and Robert L. Buchanan and Juergen Soll and Bettina B{\"o}lter},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 5},
  pages={
          2603-16
        }
}
Tic110 has been proposed to be a channel-forming protein at the inner envelope of chloroplasts whose function is essential for the import of proteins synthesized in the cytosol. Sequence features and topology determination experiments presently summarized suggest that Tic110 consists of six transmembrane helices. Its topology has been mapped by limited proteolysis experiments in combination with mass spectrometric determinations and cysteine modification analysis. Two hydrophobic transmembrane… CONTINUE READING

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