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Dual specificities of the glyoxysomal/peroxisomal processing protease Deg15 in higher plants

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Dual specificities of the glyoxysomal/peroxisomal processing protease Deg15 in higher plants

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HELM, Michael, Carsten LÜCK, Jakob PRESTELE, Georg HIERL, Pitter F. HUESGEN, Thomas FROHLICH, Georg J. ARNOLD, Iwona ADAMSKA, Angelika GÖRG, Friedrich LOTTSPEICH, Christine GIETL, 2007. Dual specificities of the glyoxysomal/peroxisomal processing protease Deg15 in higher plants. In: Proceedings of the National Academy of Sciences : PNAS. 104(27), pp. 11501-11506. ISSN 0027-8424. eISSN 1091-6490. Available under: doi: 10.1073/pnas.0704733104

@article{Helm2007speci-33171, title={Dual specificities of the glyoxysomal/peroxisomal processing protease Deg15 in higher plants}, year={2007}, doi={10.1073/pnas.0704733104}, number={27}, volume={104}, issn={0027-8424}, journal={Proceedings of the National Academy of Sciences : PNAS}, pages={11501--11506}, author={Helm, Michael and Lück, Carsten and Prestele, Jakob and Hierl, Georg and Huesgen, Pitter F. and Frohlich, Thomas and Arnold, Georg J. and Adamska, Iwona and Görg, Angelika and Lottspeich, Friedrich and Gietl, Christine} }

<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/33171"> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:contributor>Gietl, Christine</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2016-03-01T14:23:43Z</dc:date> <dc:contributor>Helm, Michael</dc:contributor> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dc:creator>Hierl, Georg</dc:creator> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dc:creator>Prestele, Jakob</dc:creator> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/33171"/> <dc:creator>Gietl, Christine</dc:creator> <dc:creator>Adamska, Iwona</dc:creator> <dc:contributor>Lottspeich, Friedrich</dc:contributor> <dc:creator>Lück, Carsten</dc:creator> <dc:contributor>Adamska, Iwona</dc:contributor> <dc:contributor>Görg, Angelika</dc:contributor> <dc:creator>Görg, Angelika</dc:creator> <dcterms:issued>2007</dcterms:issued> <dc:contributor>Huesgen, Pitter F.</dc:contributor> <dc:contributor>Lück, Carsten</dc:contributor> <dc:contributor>Frohlich, Thomas</dc:contributor> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dc:creator>Huesgen, Pitter F.</dc:creator> <dc:contributor>Hierl, Georg</dc:contributor> <dc:creator>Helm, Michael</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2016-03-01T14:23:43Z</dcterms:available> <dc:contributor>Prestele, Jakob</dc:contributor> <dcterms:abstract xml:lang="eng">Glyoxysomes are a subclass of peroxisomes involved in lipid mobilization. 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. The cleavage site typically contains a Cys at P1 or P2. We purified the glyoxysomal processing protease (GPP) from the fat-storing cotyledons of watermelon (Citrullus vulgaris) by column chromatography, preparative native isoelectric focusing, and 2D PAGE. The GPP appears in two forms, a 72-kDa monomer and a 144-kDa dimer, which are in equilibrium with one another. The equilibrium is shifted on Ca(2+) removal toward the monomer and on Ca(2+) addition toward the dimer. The monomer is a general degrading protease and is activated by denatured proteins. The dimer constitutes the processing protease because the substrate specificity proven for the monomer (Phi-Arg/Lys downward arrow) is different from the processing substrate specificity (Cys-Xxx downward arrow/Xxx-Cys downward arrow) found with the mixture of monomer and dimer. The Arabidopsis genome analysis disclosed three proteases predicted to be in peroxisomes, a Deg-protease, a pitrilysin-like metallopeptidase, and a Lon-protease. Specific antibodies against the peroxisomal Deg-protease from Arabidopsis (Deg15) identify the watermelon GPP as a Deg15. A knockout mutation in the DEG15 gene of Arabidopsis (At1g28320) prevents processing of the glyoxysomal malate dehydrogenase precursor to the mature form. Thus, the GPP/Deg15 belongs to a group of trypsin-like serine proteases with Escherichia coli DegP as a prototype. Nevertheless, the GPP/Deg15 possesses specific characteristics and is therefore a new subgroup within the Deg proteases.</dcterms:abstract> <dc:creator>Frohlich, Thomas</dc:creator> <dcterms:title>Dual specificities of the glyoxysomal/peroxisomal processing protease Deg15 in higher plants</dcterms:title> <dc:creator>Lottspeich, Friedrich</dc:creator> <dc:contributor>Arnold, Georg J.</dc:contributor> <dc:creator>Arnold, Georg J.</dc:creator> <dc:language>eng</dc:language> </rdf:Description> </rdf:RDF>

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