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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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