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JXB Advance Access published online on May 17, 2008
Journal of Experimental Botany, doi:10.1093/jxb/ern095
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© 2008 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

RESEARCH PAPER

Phosphorylation regulates the assembly of chloroplast import machinery

Mislav Oreb, Anja Höfle, Oliver Mirus and Enrico Schleiff*

JWGU Frankfurt am Main, Cluster of Excellence Macromolecular Complexes, Department of Biosciences, Max-von-Laue Str. 9, D-60439 Frankfurt, Germany

* Present address and to whom correspondence should be sent: Molecular Plant Sciences, Biocenter, N 200, 3. OG, Max-von-Laue-Str. 9, D-60438 Frankfurt/Main, Germany. E-mail: schleiff{at}bio.uni-frankfurt.de

Chloroplast function depends on the translocation of cytosolically synthesized precursor proteins into the organelle. The recognition and transfer of most precursor proteins across the outer membrane depend on a membrane inserted complex. Two receptor components of this complex, Toc34 and Toc159, are GTPases, which can be phosphorylated by kinases present in the hosting membrane. However, the physiological function of phosphorylation is not yet understood in detail. It is demonstrated that both receptors are phosphorylated within their G-domains. In vitro, the phosphorylation of Toc34 disrupts both homo- and heterodimerization of the G-domains as determined using a phospho-mimicking mutant. In endogenous membranes this mutation or phosphorylation of the wild-type receptor disturbs the association of Toc34, but not of Toc159 with the translocation pore. Therefore, phosphorylation serves as an inhibitor for the association of Toc34 with other components of the complex and phosphorylation can now be discussed as a mechanism to exchange different isoforms of Toc34 within this ensemble.

Key words: GTPase, membrane complex dynamics, phosphorylation, plastids, protein complex assembly, protein translocation, TOC

Received 29 January 2008; Revised 6 March 2008 Accepted 10 March 2008


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