Calmodulin-like protein AtCML3 mediates dimerization of peroxisomal processing protease AtDEG15 and contributes to normal peroxisome metabolism

Dolze, Esther; Chigri, Fatima; Höwing, Timo; Hierl, Georg; Isono, Erika; Vothknecht, Ute C.; Gietl, Christine

Calmodulin-like protein AtCML3 mediates dimerization of peroxisomal processing protease AtDEG15 and contributes to normal peroxisome metabolism

Dateien

Dolze_0-398984.pdfGröße: 985.99 KBDownloads: 653

Datum

2013

Autor:innen

Dolze, Esther

Chigri, Fatima

Höwing, Timo

Hierl, Georg

Isono, Erika

Vothknecht, Ute C.

Gietl, Christine

Open Access-Veröffentlichung

Open Access Hybrid

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Plant Molecular Biology. 2013, 83(6), pp. 607-624. ISSN 0167-4412. eISSN 1573-5028. Available under: doi: 10.1007/s11103-013-0112-6

Zusammenfassung

Matrix enzymes are imported into peroxisomes and glyoxysomes, a subclass of peroxisomes involved in lipid mobilization. Two peroxisomal targeting signals (PTS), the C-terminal PTS1 and the N-terminal PTS2, mediate the translocation of proteins into the organelle. PTS2 processing upon import is conserved in higher eukaryotes, and in watermelon the glyoxysomal processing protease (GPP) was shown to catalyse PTS2 processing. GPP and its ortholog, the peroxisomal DEG protease from Arabidopsis thaliana (AtDEG15), belong to the Deg/HtrA family of ATP-independent serine proteases with Escherichia coli DegP as their prototype. GPP existes in monomeric and dimeric forms. Their equilibrium is shifted towards the monomer upon Ca(2+)-removal and towards the dimer upon Ca(2+)-addition, which is accompanied by a change in substrate specificity from a general protease (monomer) to the specific cleavage of the PTS2 (dimer). We describe the Ca(2+)/calmodulin (CaM) mediated dimerization of AtDEG15. Dimerization is mediated by the CaM-like protein AtCML3 as shown by yeast two and three hybrid analyses. The binding of AtCML3 occurs within the first 25 N-terminal amino acids of AtDEG15, a domain containing a predicted CaM-binding motif. Biochemical analysis of AtDEG15 deletion constructs in planta support the requirement of the CaM-binding domain for PTS2 processing. Phylogenetic analyses indicate that the CaM-binding site is conserved in peroxisomal processing proteases of higher plants (dicots, monocots) but not present in orthologs of animals or cellular slime molds. Despite normal PTS2 processing activity, an atcml3 mutant exhibited reduced 2,4-DB sensitivity, a phenotype previously reported for the atdeg15 mutant, indicating similarly impaired peroxisome metabolism.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Schlagwörter

AtDEG15, AtCML3; Ca2+/calmodulin; Deg/HtrA serine protease; Peroxisomal processing protease

Zitieren

ISO 690

DOLZE, Esther, Fatima CHIGRI, Timo HÖWING, Georg HIERL, Erika ISONO, Ute C. VOTHKNECHT, Christine GIETL, 2013. Calmodulin-like protein AtCML3 mediates dimerization of peroxisomal processing protease AtDEG15 and contributes to normal peroxisome metabolism. In: Plant Molecular Biology. 2013, 83(6), pp. 607-624. ISSN 0167-4412. eISSN 1573-5028. Available under: doi: 10.1007/s11103-013-0112-6

BibTex

@article{Dolze2013-12Calmo-38288,
  year={2013},
  doi={10.1007/s11103-013-0112-6},
  title={Calmodulin-like protein AtCML3 mediates dimerization of peroxisomal processing protease AtDEG15 and contributes to normal peroxisome metabolism},
  number={6},
  volume={83},
  issn={0167-4412},
  journal={Plant Molecular Biology},
  pages={607--624},
  author={Dolze, Esther and Chigri, Fatima and Höwing, Timo and Hierl, Georg and Isono, Erika and Vothknecht, Ute C. and Gietl, Christine}
}

RDF

<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/server/rdf/resource/123456789/38288">
    <dc:contributor>Vothknecht, Ute C.</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-04-04T08:34:25Z</dc:date>
    <dc:creator>Vothknecht, Ute C.</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-04-04T08:34:25Z</dcterms:available>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/38288/3/Dolze_0-398984.pdf"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dcterms:issued>2013-12</dcterms:issued>
    <dcterms:abstract xml:lang="eng">Matrix enzymes are imported into peroxisomes and glyoxysomes, a subclass of peroxisomes involved in lipid mobilization. Two peroxisomal targeting signals (PTS), the C-terminal PTS1 and the N-terminal PTS2, mediate the translocation of proteins into the organelle. PTS2 processing upon import is conserved in higher eukaryotes, and in watermelon the glyoxysomal processing protease (GPP) was shown to catalyse PTS2 processing. GPP and its ortholog, the peroxisomal DEG protease from Arabidopsis thaliana (AtDEG15), belong to the Deg/HtrA family of ATP-independent serine proteases with Escherichia coli DegP as their prototype. GPP existes in monomeric and dimeric forms. Their equilibrium is shifted towards the monomer upon Ca(2+)-removal and towards the dimer upon Ca(2+)-addition, which is accompanied by a change in substrate specificity from a general protease (monomer) to the specific cleavage of the PTS2 (dimer). We describe the Ca(2+)/calmodulin (CaM) mediated dimerization of AtDEG15. Dimerization is mediated by the CaM-like protein AtCML3 as shown by yeast two and three hybrid analyses. The binding of AtCML3 occurs within the first 25 N-terminal amino acids of AtDEG15, a domain containing a predicted CaM-binding motif. Biochemical analysis of AtDEG15 deletion constructs in planta support the requirement of the CaM-binding domain for PTS2 processing. Phylogenetic analyses indicate that the CaM-binding site is conserved in peroxisomal processing proteases of higher plants (dicots, monocots) but not present in orthologs of animals or cellular slime molds. Despite normal PTS2 processing activity, an atcml3 mutant exhibited reduced 2,4-DB sensitivity, a phenotype previously reported for the atdeg15 mutant, indicating similarly impaired peroxisome metabolism.</dcterms:abstract>
    <dc:language>eng</dc:language>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:creator>Dolze, Esther</dc:creator>
    <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/38288"/>
    <dc:creator>Höwing, Timo</dc:creator>
    <dc:creator>Hierl, Georg</dc:creator>
    <dcterms:title>Calmodulin-like protein AtCML3 mediates dimerization of peroxisomal processing protease AtDEG15 and contributes to normal peroxisome metabolism</dcterms:title>
    <dc:creator>Gietl, Christine</dc:creator>
    <dc:contributor>Hierl, Georg</dc:contributor>
    <dc:creator>Isono, Erika</dc:creator>
    <dc:contributor>Gietl, Christine</dc:contributor>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/38288/3/Dolze_0-398984.pdf"/>
    <dc:creator>Chigri, Fatima</dc:creator>
    <dc:contributor>Höwing, Timo</dc:contributor>
    <dc:contributor>Chigri, Fatima</dc:contributor>
    <dc:contributor>Isono, Erika</dc:contributor>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dc:contributor>Dolze, Esther</dc:contributor>
    <dc:rights>terms-of-use</dc:rights>
  </rdf:Description>
</rdf:RDF>

Universitätsbibliographie

Nein