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Originally published In Press as doi:10.1074/jbc.M207477200 on October 3, 2002

J. Biol. Chem., Vol. 277, Issue 49, 47770-47778, December 6, 2002
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Non-canonical Transit Peptide for Import into the Chloroplast*,

Stéphane MirasDagger , Daniel SalviDagger , Myriam Ferro§, Didier Grunwald, Jérôme Garin§, Jacques JoyardDagger , and Norbert RollandDagger ||

From the Dagger  Laboratoire de Physiologie Cellulaire Végétale, UMR-5019 CNRS/CEA/Université Joseph Fourier, the § Laboratoire de Chimie des Protéines, ERM-0201 INSERM/CEA, and the  Laboratoire Canaux Ioniques et Signalisation E-9931 INSERM/CEA, Département Réponse et Dynamique Cellulaires, CEA-Grenoble, 17 rue des Martyrs, F-38054 Grenoble-cedex 9, France

The large majority of plastid proteins are nuclear-encoded and, thus, must be imported within these organelles. Unlike most of the outer envelope proteins, targeting of proteins to all other plastid compartments (inner envelope membrane, stroma, and thylakoid) is strictly dependent on the presence of a cleavable transit sequence in the precursor N-terminal region. In this paper, we describe the identification of a new envelope protein component (ceQORH) and demonstrate that its subcellular localization is limited to the inner membrane of the chloroplast envelope. Immunopurification, microsequencing of the natural envelope protein and cloning of the corresponding full-length cDNA demonstrated that this protein is not processed in the N-terminal region during its targeting to the inner envelope membrane. Transient expression experiments in plant cells were performed with truncated forms of the ceQORH protein fused to the green fluorescent protein. These experiments suggest that neither the N-terminal nor the C-terminal are essential for chloroplastic localization of the ceQORH protein. These observations are discussed in the frame of the endosymbiotic theory of chloroplast evolution and suggest that a domain of the ceQORH bacterial ancestor may have evolved so as to exclude the general requirement of an N-terminal plastid transit sequence.

* This work was supported by Génoplante Grant AF1999035 and CNRS and CEA research Programs.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains a figure and figure legend of the immunopurification of the natural spinach ceQORH protein.

|| To whom correspondence should be addressed. Tel.: 33-0-4-38-78-49-86; Fax: 33-0-4-38-78-50-91; E-mail: nrolland@cea.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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