ArticleEukaryotic cell2013
Poly(ADP-ribose) polymerase is a substrate recognized by two metacaspases of Podospora anserina.
Article in Eukaryotic cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Fungal Apoptosis-Related Proteins.Microorganisms · 2024Review
- What are the 100 most cited fungal genera?Studies in mycology · 2024Article
- Roles of CgEde1 and CgMca in Development and Virulence ofInternational journal of molecular sciences · 2024Article
- The impact of biomembranes and their dynamics on organismic aging: insights from a fungal aging model.Frontiers in aging · 2024Review
- Insights on Novel Effectors and Characterization of Metacaspase (RS107_6) as a Potential Cell Death-Inducing Protein inMicroorganisms · 2023Article
- Regulating Death and Disease: Exploring the Roles of Metacaspases in Plants and Fungi.International journal of molecular sciences · 2022Review
- A Network of Pathways Controlling Cellular Homeostasis Affects the Onset of Senescence inJournal of fungi (Basel, Switzerland) · 2021Review
- Impaired FCells · 2021Article
- Cutting Out the Gaps Between Proteases and Programmed Cell Death.Frontiers in plant science · 2019Article
- Structural and functional diversity of caspase homologues in non-metazoan organisms.Protoplasma · 2018Review
- Metacaspases versus caspases in development and cell fate regulation.Cell death and differentiation · 2017Review
- Regulated Forms of Cell Death in Fungi.Frontiers in microbiology · 2017Review
- Cyclophilin D Is Involved in the Regulation of Autophagy and Affects the Lifespan of P. anserina in Response to Mitochondrial Oxidative Stress.Frontiers in genetics · 2016Article
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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
The two metacaspases MCA1 and MCA2 of the fungal aging model organism Podospora anserina (PaMCA1 and PaMCA2, respectively) have previously been demonstrated to be involved in the control of programmed cell death (PCD) and life span. In order to identify specific pathways and components which are controlled by the activity of these enzymes, we set out to characterize them further. Heterologous overexpression in Escherichia coli of the two metacaspase genes resulted in the production of proteins which aggregate and form inclusion bodies from which the active protein has been recovered via refolding in appropriate buffers. The renaturated proteins are characterized by an arginine-specific activity and are active in caspase-like self-maturation leading to the generation of characteristic small protein fragments. Both activities are dependent on the presence of calcium. Incubation of the two metacaspases with recombinant poly(ADP-ribose) polymerase (PARP), a known substrate of mammalian caspases, led to the identification of PARP as a substrate of the two P. anserina proteases. Using double mutants in which P. anserina Parp (PaParp) is overexpressed and PaMca1 is either overexpressed or deleted, we provide evidence for in vivo degradation of PaPARP by PaMCA1. These results support the idea that the substrate profiles of caspases and metacaspases are at least partially overlapping. Moreover, they link PCD and DNA maintenance in the complex network of molecular pathways involved in aging and life span control.
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