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Research article

Substrate binding disrupts dimerization and induces nucleotide exchange of the chloroplast GTPase Toc33

Mislav Oreb, Anja Höfle, Patrick Koenig, Maik S. Sommer, Irmgard Sinning, Fei Wang, Ivo Tews, Danny J. Schnell, Enrico Schleiff
Biochemical Journal May 13, 2011, 436 (2) 313-319; DOI: 10.1042/BJ20110246
Mislav Oreb
Center for Membrane Proteomics and the Cluster of Excellence Frankfurt, Department of Biosciences, Molecular Cell Biology of Plants, Goethe University Frankfurt, Max-von-Laue Str. 8, D-60438 Frankfurt am Main, Germany
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Anja Höfle
Center for Membrane Proteomics and the Cluster of Excellence Frankfurt, Department of Biosciences, Molecular Cell Biology of Plants, Goethe University Frankfurt, Max-von-Laue Str. 8, D-60438 Frankfurt am Main, Germany
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Patrick Koenig
Biochemistry Center (BZH), Heidelberg University, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany
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Maik S. Sommer
Center for Membrane Proteomics and the Cluster of Excellence Frankfurt, Department of Biosciences, Molecular Cell Biology of Plants, Goethe University Frankfurt, Max-von-Laue Str. 8, D-60438 Frankfurt am Main, Germany
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Irmgard Sinning
Biochemistry Center (BZH), Heidelberg University, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany
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Fei Wang
Department of Biochemistry and Molecular Biology, University of Massachusetts, 710 North Pleasant Street, Amherst, MA 01003, U.S.A.
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Ivo Tews
Biochemistry Center (BZH), Heidelberg University, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany
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Danny J. Schnell
Department of Biochemistry and Molecular Biology, University of Massachusetts, 710 North Pleasant Street, Amherst, MA 01003, U.S.A.
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Enrico Schleiff
Center for Membrane Proteomics and the Cluster of Excellence Frankfurt, Department of Biosciences, Molecular Cell Biology of Plants, Goethe University Frankfurt, Max-von-Laue Str. 8, D-60438 Frankfurt am Main, Germany
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  • For correspondence: schleiff@bio.uni-frankfurt.de
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This article has a commentary. Please see:

  • Dimerization of TOC receptor GTPases and its implementation for the control of protein import into chloroplasts

Abstract

GTPases act as molecular switches to control many cellular processes, including signalling, protein translation and targeting. Switch activity can be regulated by external effector proteins or intrinsic properties, such as dimerization. The recognition and translocation of pre-proteins into chloroplasts [via the TOC/TIC (translocator at the outer envelope membrane of chloroplasts/inner envelope membrane of chloroplasts)] is controlled by two homologous receptor GTPases, Toc33 and Toc159, whose reversible dimerization is proposed to regulate translocation of incoming proteins in a GTP-dependent manner. Toc33 is a homodimerizing GTPase. Functional analysis suggests that homodimerization is a key step in the translocation process, the molecular functions of which, as well as the elements regulating this event, are largely unknown. In the present study, we show that homodimerization reduces the rate of nucleotide exchange, which is consistent with the observed orientation of the monomers in the crystal structure. Pre-protein binding induces a dissociation of the Toc33 homodimer and results in the exchange of GDP for GTP. Thus homodimerization does not serve to activate the GTPase activity as discussed many times previously, but to control the nucleotide-loading state. We discuss this novel regulatory mode and its impact on the current models of protein import into the chloroplast.

  • dimeric GTPase
  • GDP-dissociation-inhibitor function (GDI function)
  • G-protein
  • protein translocation
  • substrate-based regulation

Abbreviations: EDA-GTP-ATTO-550, 2′/3′-O-(2-aminoethyl-carbamoyl)-GTP labelled with ATTO-550, triethylammonium salt; GAD, G-protein activated by nucleotide-dependent dimerization; GAP, GTPase-activating protein; GDI, GDP-dissociation inhibitor; GDF, GDI-displacement factor; mantGDP, 2′/3′-O-(N-methylanthraniloyl)-GDP, triethylammonium salt; Rubisco, ribulose-1,5-bisphosphate carboxylase/oxygenase; pSSU, precursor of the small subunit of Rubisco; TOC/Toc, translocator at the outer envelope membrane of chloroplasts

  • © The Authors Journal compilation © 2011 Biochemical Society
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June 2011

Volume: 436 Issue: 2

Biochemical Journal: 436 (2)
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Substrate binding disrupts dimerization and induces nucleotide exchange of the chloroplast GTPase Toc33
Mislav Oreb, Anja Höfle, Patrick Koenig, Maik S. Sommer, Irmgard Sinning, Fei Wang, Ivo Tews, Danny J. Schnell, Enrico Schleiff
Biochemical Journal Jun 2011, 436 (2) 313-319; DOI: 10.1042/BJ20110246
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Substrate binding disrupts dimerization and induces nucleotide exchange of the chloroplast GTPase Toc33
Mislav Oreb, Anja Höfle, Patrick Koenig, Maik S. Sommer, Irmgard Sinning, Fei Wang, Ivo Tews, Danny J. Schnell, Enrico Schleiff
Biochemical Journal Jun 2011, 436 (2) 313-319; DOI: 10.1042/BJ20110246

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Keywords

dimeric GTPase
GDP-dissociation-inhibitor function (GDI function)
G-protein
protein translocation
substrate-based regulation

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