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Arabidopsis Tic62 and Ferredoxin-NADP(H) Oxidoreductase Form Light-Regulated Complexes That Are Integrated into the Chloroplast Redox Poise

J.P. Benz, A. Stengel, M. Lintala, Y.-H. Lee, A. Weber, K. Philippar, I.L. Gügel, S. Kaieda, T. Ikegami, P. Mulo, J. Soll, B. Bölter
J.P. Benz
aMunich Center for Integrated Protein Science CiPSM, Ludwig-Maximilians-Universität München, D-81377 Munich, Germany
bDepartment of Biology I, Botany, Ludwig-Maximilians-Universität München, D-82152 Planegg-Martinsried, Germany
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A. Stengel
aMunich Center for Integrated Protein Science CiPSM, Ludwig-Maximilians-Universität München, D-81377 Munich, Germany
bDepartment of Biology I, Botany, Ludwig-Maximilians-Universität München, D-82152 Planegg-Martinsried, Germany
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M. Lintala
cLaboratory of Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014 Turku, Finland
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Y.-H. Lee
dInstitute for Protein Research, Osaka University and CREST, Japan Science and Technology Agency, Suita, Osaka 565-0871, Japan
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A. Weber
eInstitut für Biochemie der Pflanzen, Heinrich-Heine-Universität, 40225 Duesseldorf, Germany
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K. Philippar
aMunich Center for Integrated Protein Science CiPSM, Ludwig-Maximilians-Universität München, D-81377 Munich, Germany
bDepartment of Biology I, Botany, Ludwig-Maximilians-Universität München, D-82152 Planegg-Martinsried, Germany
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I.L. Gügel
aMunich Center for Integrated Protein Science CiPSM, Ludwig-Maximilians-Universität München, D-81377 Munich, Germany
bDepartment of Biology I, Botany, Ludwig-Maximilians-Universität München, D-82152 Planegg-Martinsried, Germany
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S. Kaieda
dInstitute for Protein Research, Osaka University and CREST, Japan Science and Technology Agency, Suita, Osaka 565-0871, Japan
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T. Ikegami
dInstitute for Protein Research, Osaka University and CREST, Japan Science and Technology Agency, Suita, Osaka 565-0871, Japan
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P. Mulo
cLaboratory of Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014 Turku, Finland
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J. Soll
aMunich Center for Integrated Protein Science CiPSM, Ludwig-Maximilians-Universität München, D-81377 Munich, Germany
bDepartment of Biology I, Botany, Ludwig-Maximilians-Universität München, D-82152 Planegg-Martinsried, Germany
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B. Bölter
aMunich Center for Integrated Protein Science CiPSM, Ludwig-Maximilians-Universität München, D-81377 Munich, Germany
bDepartment of Biology I, Botany, Ludwig-Maximilians-Universität München, D-82152 Planegg-Martinsried, Germany
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Published December 2009. DOI: https://doi.org/10.1105/tpc.109.069815

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Abstract

Translocation of nuclear-encoded preproteins across the inner envelope of chloroplasts is catalyzed by the Tic translocon, consisting of Tic110, Tic40, Tic62, Tic55, Tic32, Tic20, and Tic22. Tic62 was proposed to act as a redox sensor of the complex because of its redox-dependent shuttling between envelope and stroma and its specific interaction with the photosynthetic protein ferredoxin-NADP(H) oxidoreductase (FNR). However, the nature of this close relationship so far remained enigmatic. A putative additional localization of Tic62 at the thylakoids mandated further studies examining how this feature might be involved in the respective redox sensing pathway and the interaction with its partner protein. Therefore, both the association with FNR and the physiological role of the third, thylakoid-bound pool of Tic62 were investigated in detail. Coexpression analysis indicates that Tic62 has similar expression patterns as genes involved in photosynthetic functions and protein turnover. At the thylakoids, Tic62 and FNR form high molecular weight complexes that are not involved in photosynthetic electron transfer but are dynamically regulated by light signals and the stromal pH. Structural analyses reveal that Tic62 binds to FNR in a novel binding mode for flavoproteins, with a major contribution from hydrophobic interactions. Moreover, in absence of Tic62, membrane binding and stability of FNR are drastically reduced. We conclude that Tic62 represents a major FNR interaction partner not only at the envelope and in the stroma, but also at the thylakoids of Arabidopsis thaliana and perhaps all flowering plants. Association with Tic62 stabilizes FNR and is involved in its dynamic and light-dependent membrane tethering.

  • Received July 6, 2009.
  • Revised October 29, 2009.
  • Accepted December 14, 2009.
  • Published December 29, 2009.
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Arabidopsis Tic62 and Ferredoxin-NADP(H) Oxidoreductase Form Light-Regulated Complexes That Are Integrated into the Chloroplast Redox Poise
J.P. Benz, A. Stengel, M. Lintala, Y.-H. Lee, A. Weber, K. Philippar, I.L. Gügel, S. Kaieda, T. Ikegami, P. Mulo, J. Soll, B. Bölter
The Plant Cell Dec 2009, 21 (12) 3965-3983; DOI: 10.1105/tpc.109.069815

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Arabidopsis Tic62 and Ferredoxin-NADP(H) Oxidoreductase Form Light-Regulated Complexes That Are Integrated into the Chloroplast Redox Poise
J.P. Benz, A. Stengel, M. Lintala, Y.-H. Lee, A. Weber, K. Philippar, I.L. Gügel, S. Kaieda, T. Ikegami, P. Mulo, J. Soll, B. Bölter
The Plant Cell Dec 2009, 21 (12) 3965-3983; DOI: 10.1105/tpc.109.069815
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The Plant Cell Online: 21 (12)
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Vol. 21, Issue 12
December 2009
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