An Arabidopsis Mutant Defective in the Plastid General Protein Import Apparatus

Author:

Jarvis Paul1,Chen Lih-Jen1,Li Hsou-min1,Peto Charles A.1,Fankhauser Christian1,Chory Joanne1

Affiliation:

1. P. Jarvis and C. Fankhauser, Plant Biology Laboratory, Salk Institute, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA. L.-J. Chen and H.-m. Li, Institute of Molecular Biology, Academia Sinica, Nankang, Taipei 11529, Taiwan. C. A. Peto, Laboratory of Neuronal Structure and Function, Salk Institute, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA. J. Chory, Plant Biology Laboratory and Howard Hughes Medical Institute, Salk Institute, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA.

Abstract

Elaborate mechanisms have evolved for the translocation of nucleus-encoded proteins across the plastid envelope membrane. Although putative components of the import apparatus have been identified biochemically, their role in import remains to be proven in vivo. An Arabidopsis mutant lacking a new component of the import machinery [translocon at the outer envelope membrane of chloroplasts (Toc33), a 33-kilodalton protein] has been isolated. The functional similarity of Toc33 to another translocon component (Toc34) implies that multiple different translocon complexes are present in plastids. Processes that are mediated by Toc33 operate during the early stages of plastid and leaf development. The data demonstrate the in vivo role of a translocon component in plastid protein import.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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