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Published 23 July 2001. doi:10.1083/jcb.200104022
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© The Rockefeller University Press, 0021-9525/2001/7/309 $5.00
The Journal of Cell Biology, Volume 154, Number 2, July 23, 2001 309-316


Article

Targeting of an abundant cytosolic form of the protein import receptor at Toc159 to the outer chloroplast membrane



Andreas Hiltbrunner1, Jörg Bauer1, Pierre-Alexandre Vidi1, Sibylle Infanger1, Petra Weibel1, Morten Hohwy2 and Felix Kessler1

1 Institute of Plant Sciences, Plant Physiology and Biochemistry Group, 8092 Zürich, Switzerland
2 Institute of Molecular Biology and Biophysics, 8093 Zürich, Switzerland

Address correspondence to Felix Kessler, Institute of Plant Sciences, Plant Physiology and Biochemistry Group, ETH Zürich, Universitätstrasse 2, 8092 Zürich, Switzerland. Tel.: 41-1-632-60-15. Fax: 41-1-632-10-84. E-mail: felix.kessler{at}ipw.biol.ethz.ch

Chloroplast biogenesis requires the large-scale import of cytosolically synthesized precursor proteins. A trimeric translocon (Toc complex) containing two homologous GTP-binding proteins (atToc33 and atToc159) and a channel protein (atToc75) facilitates protein translocation across the outer envelope membrane. The mechanisms governing function and assembly of the Toc complex are not yet understood. This study demonstrates that atToc159 and its pea orthologue exist in an abundant, previously unrecognized soluble form, and partition between cytosol-containing soluble fractions and the chloroplast outer membrane. We show that soluble atToc159 binds directly to the cytosolic domain of atToc33 in a homotypic interaction, contributing to the integration of atToc159 into the chloroplast outer membrane. The data suggest that the function of the Toc complex involves switching of atToc159 between a soluble and an integral membrane form.

Key Words: chloroplasts; protein import; translocon; complex assembly; soluble receptor


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