ArticleThe New phytologist2018
Type III metacaspases: calcium-dependent activity proposes new function for the p10 domain.
Article in The New phytologist, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Apoptotic bodies in phytoplankton suggest evolutionary conservation of cell death mechanisms.Nature communications · 2025Article
- Structural determinants for pH-dependent activation of a plant metacaspase.Nature communications · 2025Article
- Type II metacaspase mediates light-dependent programmed cell death in Chlamydomonas reinhardtii.Plant physiology · 2024Article
- Differential Expression of Stress Adaptation Genes in a DiatomInternational journal of molecular sciences · 2024Article
- Structure-function study of a CaProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Vacuolar Processing Enzymes in Plant Programmed Cell Death and Autophagy.International journal of molecular sciences · 2023Review
- Regulating Death and Disease: Exploring the Roles of Metacaspases in Plants and Fungi.International journal of molecular sciences · 2022Review
- Article
- Plant cell responses to allelopathy: from oxidative stress to programmed cell death.Protoplasma · 2022Review
- Evolutionary Diversity and Function of Metacaspases in Plants: Similar to but Not Caspases.International journal of molecular sciences · 2022Review
- Expression and Purification of the Type I Metacaspase from a Cryptophyte Guillardia theta , GtMCA-I.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Expression and Purification of the Type II Metacaspase from a Unicellular Green Alga Chlamydomonas reinhardtii.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Biochemical Characterization of a Novel Redox-Regulated Metacaspase in a Marine Diatom.Frontiers in microbiology · 2021Article
- Cell Death in Cyanobacteria: Current Understanding and Recommendations for a Consensus on Its Nomenclature.Frontiers in microbiology · 2021Review
- Identification and characterization ofBiochemistry and biophysics reports · 2019Article
- Phylogenetic Distribution and Diversity of Bacterial Pseudo-Orthocaspases Underline Their Putative Role in Photosynthesis.Frontiers in plant science · 2019Article
- Structural and functional diversity of caspase homologues in non-metazoan organisms.Protoplasma · 2018Review
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No grant is acknowledged in the PubMed record.
Abstract
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.
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