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Plant Physiol, April 2001, Vol. 125, pp. 1567-1576

Arabidopsis Genes Encoding Components of the Chloroplastic Protein Import Apparatus1

Diane Jackson-Constan and Kenneth Keegstra*

Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824-1312

The process of protein import into plastids has been studied extensively using isolated pea (Pisum sativum) chloroplasts. As a consequence, virtually all of the known components of the proteinaceous apparatus that mediates import were originally cloned from pea. With the recent completion of the Arabidopsis genome sequencing project, it is now possible to identify putative homologs of the import components in this species. Our analysis has revealed that Arabidopsis homologs with high sequence similarity exist for all of the pea import complex subunits, making Arabidopsis a valid model for further study of this system. Multiple homologs can be identified for over one-half of the components. In all but one case it is known that more than one of the putative isoforms for a particular subunit are expressed. Thus, it is possible that multiple types of import complexes are present within the same cell, each having a unique affinity for different chloroplastic precursor proteins, depending upon the exact mix of isoforms it contains. Sequence analysis of the putative Arabidopsis homologs for the chloroplast protein import apparatus has revealed many questions concerning subunit function and evolution. It should now be possible to use the genetic tools available in Arabidopsis, including the generation of knockout mutants and antisense technology, to address these questions and learn more about the molecular functions of each of the components during the import process.


1 This work was supported in part by the Division of Energy Biosciences at the U.S. Department of Energy (grants to K.K.), by the Cell Biology Program at the National Science Foundation (to K.K.), and by the Graduate Fellowship Program at the National Science Foundation (to D.J.-C.).

* Corresponding author; e-mail keegstra{at}msu.edu; fax 517-353-9168.

© 2001 American Society of Plant Physiologists



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