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Published online 2 December 2002. doi:10.1083/jcb.200208018
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© The Rockefeller University Press, 0021-9525/2002/12/845 $5.00
The Journal of Cell Biology, Volume 159, Number 5, 845-854

Article

 Essential role of the G-domain in targeting of the protein import receptor atToc159 to the chloroplast outer membrane

Jörg Bauer3, Andreas Hiltbrunner1, Petra Weibel1, Pierre-Alexandre Vidi1, Mayte Alvarez-Huerta1, Matthew D. Smith2, Danny J. Schnell2 and Felix Kessler1

1 Plant Physiology and Biochemistry Group, Institute of Plant Sciences, ETH Zürich, CH-8092 Zürich, Switzerland
2 Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA 01003
3 BASF Plant Science GmbH, 67056 Ludwigshafen, Germany

Address correspondence to Felix Kessler, Institut de Botanique, Laboratoire de Physiologie Végétale, Université de Neuchâtel, Rue Emile-Argand 11, CH-2007 Neuchâtel, Switzerland. Tel.: 41-32-718-22-92. Fax: 41-32-718-22-71. E-mail: felix.kessler{at}unine.ch

Two homologous GTP-binding proteins, atToc33 and atToc159, control access of cytosolic precursor proteins to the chloroplast. atToc33 is a constitutive outer chloroplast membrane protein, whereas the precursor receptor atToc159 also exists in a soluble, cytosolic form. This suggests that atToc159 may be able to switch between a soluble and an integral membrane form. By transient expression of GFP fusion proteins, mutant analysis, and biochemical experimentation, we demonstrate that the GTP-binding domain regulates the targeting of cytosolic atToc159 to the chloroplast and mediates the switch between cytosolic and integral membrane forms. Mutant atToc159, unable to bind GTP, does not reinstate a green phenotype in an albino mutant (ppi2) lacking endogenous atToc159, remaining trapped in the cytosol. Thus, the function of atToc159 in chloroplast biogenesis is dependent on an intrinsic GTP-regulated switch that controls localization of the receptor to the chloroplast envelope.

Key Words: Arabidopsis; chloroplast biogenesis; molecular switch; receptor targeting; GTP


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