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Type III metacaspases: calcium-dependent activity proposes new function for the p10 domain
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry. Department of Chemistry and Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, Vecna pot 113, SI-1000 Ljubljana, Slovenia.
2018 (English)In: New Phytologist, ISSN 0028-646X, E-ISSN 1469-8137, Vol. 218, no 3 Special issue, p. 1179-1191Article in journal (Refereed) Published
Abstract [en]

Metacaspases are a subgroup of caspase homologues represented in bacteria, algae and plants. Although type I and type II metacaspases are present in plants, recently discovered and uncharacterized type III metacaspases can only be found in algae which have undergone secondary endosymbiosis. We analysed the expression levels of all 13 caspase homologues in the cryptophyte Guillardia theta in vivo and biochemically characterized its only type III metacaspase, GtMC2, in vitro. Type III metacaspase GtMC2 was shown to be an endopeptidase with a preference for basic amino acids in the P1 position, which exhibited specific N-terminal proteolytic cleavage for full catalytic efficiency. Autolytic processing, as well as the activity of the mature enzyme, required the presence of calcium ions in low millimolar concentrations. In GtMC2, two calcium-binding sites were identified, one with a dissociation constant at low and the other at high micromolar concentrations. We show high functional relatedness of type III metacaspases to type I metacaspases. Moreover, our data suggest that the low-affinity calcium-binding site is located in the p10 domain, which contains a well-conserved N-terminal region. This region can only be found in type I/II/III metacaspases, but is absent in calcium-independent caspase homologues.

Place, publisher, year, edition, pages
Hoboken: John Wiley & Sons, 2018. Vol. 218, no 3 Special issue, p. 1179-1191
Keywords [en]
algae, caspase, cryptophyte, programmed cell death, proteolysis
National Category
Chemical Sciences Plant Biotechnology
Identifiers
URN: urn:nbn:se:umu:diva-143746DOI: 10.1111/nph.14660ISI: 000430127000029OAI: oai:DiVA.org:umu-143746DiVA, id: diva2:1171619
Available from: 2018-01-08 Created: 2018-01-08 Last updated: 2018-06-13Bibliographically approved

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Klemenčič, MarinaFunk, Christiane

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