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Plant and Cell Physiology Advance Access published online on April 11, 2005
Plant and Cell Physiology, doi:10.1093/pcp/pci107
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Plant and Cell Physiology 2005 © The Japanese Society of Plant Physiologists (JSPP); all rights reserved.
Received February 23, 2005
Accepted April 7, 2005

Regular Paper

Catalysis, Subcellular Localization, Expression and Evolution of the Targeting Peptides Degrading Protease, AtPreP2

Shashi Bhushan 1, Annelie Ståhl 1, Stefan Nilsson 1, Benoit Lefebvre 2, Motoaki Seki 3, Christian Roth 4, David McWilliam 5, Sarah J. Wright 6, David A. Liberles 4, Kazuo Shinozaki 3, Barry D. Bruce 7, Marc Boutry 2, and Elzbieta Glaser 1*

1 Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, 10691 Stockholm, Sweden
2 Unité de Biochimie Physiologique, Institut des sciences de la vie, Université Catholique de Louvain de Louvain, Croix du Sud, 2-20, B-1348 Louvain-la-Neuve, Belgium
3 Plant Functional Genomic Research Group, RIKEN GSC, Japan
4 Computational Biology Unit, BCCS, University of Bergen, 5020 Bergen, Norway
5 Graduate Program in Genome Science and Technology, University of Tennessee, Knoxville, TN 37996 USA
6 Center of Excellence in Structural Biology, Department of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996 USA
7 Graduate Program in Genome Science and Technology, University of Tennessee, Knoxville, TN 37996 USA; Center of Excellence in Structural Biology, Department of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996 USA

* To whom correspondence should be addressed.
Elzbieta Glaser, E-mail: e_glaser{at}dbb.su.se


  Abstract

We have previously identified a zinc metalloprotease involved in the degradation of mitochondrial and chloroplast targeting peptides, the Presequence Protease (PreP). In the Arabidopsis thaliana genomic database there are two genes that correspond to the protease, the zinc-metalloprotease (AAL90904) and the putative zinc-metalloprotease (AAG13049). We have named the corresponding proteins AtPreP1 and AtPreP2, respectively. AtPreP1 and AtPreP2 show significant differences in their targeting peptides and the proteins are predicted to be localized in different compartments. AtPreP1 was shown to degrade both mitochondrial and chloroplast targeting peptides and to be dual-targeted to both organelles using an ambiguous targeting peptide. Here, we have overexpressed, purified and characterized proteolytic and targeting properties of AtPreP2. AtPreP2 exhibits different proteolytic subsite specificity than AtPreP1 when used for degradation of organellar targeting peptides and their mutants. Interestingly, AtPreP2 precursor protein was also found to be dual-targeted to both mitochondria and chloroplasts in a single and dual in vitro import system. Furthermore, targeting peptide of the AtPreP2 dually targeted GFP to both mitochondria and chloroplasts in tobacco protoplasts and leaves using an in vivo transient expression system. The targeting of both AtPreP1 and AtPreP2 proteases to chloroplasts in A. thaliana in vivo was confirmed via a shotgun mass spectrometric analysis of highly purified chloroplasts. RT-PCR analysis revealed that AtPreP1 and AtPreP2 are differentially expressed in the mature A. thaliana plants. Phylogenetic evidence indicated that AtPreP1 and AtPreP2 are recent gene duplicates that may have diverged through subfunctionalization.

Keywords: Chloroplasts; Dual targeting; Mitochondria; Presequence Protease; Protein import; Zinc metalloprotease.
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