ArticleCell death & disease2013
New types of metacaspases in phytoplankton reveal diverse origins of cell death proteases.
Article in Cell death & disease, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 126 citations in OpenAlex.
- Regulated Cell Death in Fungi, the Role of Metacaspases and Assay Techniques.Methods and protocols · 2026Review
- Metacaspases contribute to the cellular response to heat stress in a marine diatom.The New phytologist · 2026Article
- Cell death is a conserved innate disease resistance response of brown algae against the oomyceteiScience · 2025Article
- Cysteine proteases and how YabG fits into clan CD of the MEROPS database.Journal of bacteriology · 2025Review
- Structural determinants for pH-dependent activation of a plant metacaspase.Nature communications · 2025Article
- Solving Challenges in Microalgae-Based Living Materials.ACS synthetic biology · 2025Article
- Type II metacaspase mediates light-dependent programmed cell death in Chlamydomonas reinhardtii.Plant physiology · 2024Article
- Expansion and diversity of caspases in Mytilus coruscus contribute to larval metamorphosis and environmental adaptation.BMC genomics · 2024Review
- Thermoprotection by a cell membrane-localized metacaspase in a green alga.The Plant cell · 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
- Regulating Death and Disease: Exploring the Roles of Metacaspases in Plants and Fungi.International journal of molecular sciences · 2022Review
- Article
- In silico insight of cell-death-related proteins in photosynthetic cyanobacteria.Archives of microbiology · 2022Review
- Evolutionary Diversity and Function of Metacaspases in Plants: Similar to but Not Caspases.International journal of molecular sciences · 2022Review
- The Ancient Origins of Death Domains Support the 'Original Sin' Hypothesis for the Evolution of Programmed Cell Death.Journal of molecular evolution · 2022Article
- Expression and Purification of the Type I Metacaspase from a Cryptophyte Guillardia theta , GtMCA-I.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Identification of a Metacaspase Gene in the Bloom-Forming Dinoflagellate Prorocentrum minimum and its Putative Function Involved in Programmed Cell Death.Current microbiology · 2021Article
- Cell Death and Metabolic Stress inToxins · 2021Article
- Integrated RNA-seq and Proteomic Studies Reveal Resource Reallocation towards Energy Metabolism and Defense inApplied and environmental microbiology · 2021Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Metacaspases are evolutionarily distant homologs of caspases that are found outside the metazoan and are known to have key roles in programmed cell death (PCD). Two types of metacaspases (types I and II) have been defined in plants based on their domain structures; these have similarities to metazoan 'initiator' and 'executioner' caspases. However, we know little about metacaspases in unicellular organisms and even less about their roles in cell death. We identified a novel group of metacaspases in sequenced phytoplanktonic protists that show domain architectures distinct from either type I or II enzymes; we designate them as type III. Type III metacaspases exhibit a rearrangement of domain structures between N- and C-terminus. In addition, we found a group of metacaspase-like proteases in phytoplankton that show sequence homology with other metacaspases, but defy classification in conventional schemes. These metacaspase-like proteases exist in bacteria alongside a variant of type I metacaspases and we propose these bacterial metacaspases are the origins of eukaryotic metacaspases. Type II and III metacaspases were not detected in bacteria and they might be variants of bacterial type I metacaspases that evolved in plants and phytoplanktonic protists, respectively, during the establishment of plastids through the primary and secondary endosymbiotic events. A complete absence of metacaspases in protists that lost plastids, such as oömycetes and ciliates indicates the gene loss during the plastid-to-nucleus gene transfer. Taken together, our findings suggest endosymbiotic gene transfer (EGT) is a key mechanism resulting in the evolutionary diversity of cell death proteases.
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