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Published on October 24, 2008; 10.1104/pp.108.125377

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Received June 26, 2008
Accepted October 20, 2008

The DEG15 Serine Protease Cleaves Peroxisomal Targeting Signal 2-Containing Proteins in Arabidopsis thaliana

Holger Schuhmann , Pitter F. Huesgen , Christine Gietl , and Iwona Adamska *

Department of Physiology and Plant Biochemistry, University of Konstanz, Universitatsstrasse 10, DE-78457 Konstanz, Germany; Biologikum Weihenstephan, Technical University of Munich, Am Hochanger 4, DE-85350 Freising, Germany

* Corresponding author; email: iwona.adamska{at}uni-konstanz.de.

Two distinct peroxisomal targeting signals (PTSs), the C-terminal PTS1 and the N-terminal PTS2, are defined. Processing of the PTS2 on protein import is conserved in higher eukaryotes. Recently, candidates for the responsible processing protease were identified from plants (DEG15) and mammals (TYSND1). We demonstrate that plants lacking DEG15 show an expressed phenotype potentially linked to reduced {beta}-oxidation, indicating for the first time the impact of protein processing on peroxisomal functions in higher eukaryotes. Mutational analysis of Arabidopsis (Arabidopsis thaliana) DEG15 revealed that conserved histidine, aspartate, and serine residues are essential for the proteolytic activity of this enzyme in vitro. This indicates that DEG15 and related enzymes are trypsin-like serine endopeptidases. Deletion of a plant-specific stretch present in the protease domain diminished but not abolished the proteolytic activity of DEG15 against the PTS2-containing glyoxysomal malate dehydrogenase. Fluorescence microscopy showed that a DEG15-green fluorescent protein fusion construct is targeted to peroxisomes in planta. In vivo studies with isolated homozygous deg15 knock-out mutants and complemented mutant lines suggest that this enzyme mediates general processing of PTS2-containing proteins




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M. J. Lingard and B. Bartel
Arabidopsis LON2 Is Necessary for Peroxisomal Function and Sustained Matrix Protein Import
Plant Physiology, November 1, 2009; 151(3): 1354 - 1365.
[Abstract] [Full Text] [PDF]


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