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JXB Advance Access published online on November 14, 2008
Journal of Experimental Botany, doi:10.1093/jxb/ern283
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© The Author [2008]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

RESEARCH PAPER

In vivo interaction between atToc33 and atToc159 GTP-binding domains demonstrated in a plant split-ubiquitin system

Gwendoline Rahim1, Sylvain Bischof2, Felix Kessler1 and Birgit Agne1,*

1Laboratoire de Physiologie Végétale, Institut de Biologie, Université de Neuchâtel, Rue Emile-Argand 11, CH-2009 Neuchâtel, Switzerland
2Institute of Plant Sciences, ETH Zurich, Universitätstrasse 2, Zurich, Switzerland

* To whom correspondence should be addressed. E-mail: birgit.agne{at}unine.ch

The GTPases atToc33 and atToc159 are pre-protein receptor components of the translocon complex at the outer chloroplast membrane in Arabidopsis. Despite their participation in the same complex in vivo, evidence for their interaction is still lacking. Here, a split-ubiquitin system is engineered for use in plants, and the in vivo interaction of the Toc GTPases in Arabidopsis and tobacco protoplasts is shown. Using the same method, the self-interaction of the peroxisomal membrane protein atPex11e is demonstrated. The finding suggests a more general suitability of the split-ubiquitin system as a plant in vivo interaction assay.

Key words: Heterodimerization, in vivo, protein–protein interaction, protoplast, split-ubiquitin, Toc GTPases

Received 12 August 2008; Revised 18 October 2008 Accepted 20 October 2008


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