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Updated: Sep 1, 2025

Measuring Calpain Activity in Fixed and Living Cells by Flow Cytometry
Published on: July 8, 2010
Calpains in cyanobacteria and the origin of calpains
Dominika Vešelényiová1, Lenka Hutárová2, Alexandra Lukáčová3
1Department of Biology, Faculty of Natural Sciences, University of Ss. Cyril and Methodius in Trnava, Námestie J. Herdu 577/2, 917 01, Trnava, Slovakia. dominika.veselenyiova@ucm.sk.
Abstract:
Calpains are cysteine proteases involved in many cellular processes. They are an ancient and large superfamily of enzymes responsible for the cleavage and irreversible modification of a large variety of substrates. They have been intensively studied in humans and other mammals, but information about calpains in bacteria is scarce. Calpains have not been found among Archaea to date. In this study, we have investigated the presence of calpains in selected cyanobacterial species using in silico analyses. We show that calpains defined by possessing CysPC core domain are present in cyanobacterial genera Anabaena, Aphanizomenon, Calothrix, Chamaesiphon, Fischerella, Microcystis, Scytonema and Trichormus. Based on in silico protein interaction analysis, we have predicted putative interaction partners for identified cyanobacterial calpains. The phylogenetic analysis including cyanobacterial, other bacterial and eukaryotic calpains divided bacterial and eukaryotic calpains into two separate monophyletic clusters. We propose two possible evolutionary scenarios to explain this tree topology: (1) the eukaryotic ancestor or an archaeal ancestor of eukaryotes obtained calpain gene from an unknown bacterial donor, or alternatively (2) calpain gene had been already present in the last common universal ancestor and subsequently lost by the ancestor of Archaea, but retained by the ancestor of Bacteria and by the ancestor of Eukarya. Both scenarios would require multiple independent losses of calpain genes in various bacteria and eukaryotes.
Insights
Calpains, cysteine proteases, are found in several cyanobacteria genera. Phylogenetic analysis suggests calpains may have originated in the last universal common ancestor or were acquired by eukaryotes from bacteria.
Area of Science:
- Biochemistry
- Molecular Biology
- Evolutionary Biology
Background:
- Calpains are a large superfamily of cysteine proteases crucial for numerous cellular functions.
- While extensively studied in mammals, calpain presence and function in bacteria remain largely unexplored.
- Archaea have not been found to possess calpains.
Purpose of the Study:
- To investigate the presence and evolutionary origins of calpains in cyanobacteria.
- To identify potential interaction partners for cyanobacterial calpains.
- To elucidate the evolutionary history of calpains across different domains of life.
Main Methods:
- In silico analyses were employed to identify calpains within selected cyanobacterial genomes.
- Protein-protein interaction analyses were performed to predict putative interaction partners.
- Phylogenetic analyses were conducted using calpain sequences from cyanobacteria, other bacteria, and eukaryotes.
Main Results:
- Calpains, characterized by the CysPC core domain, were identified in multiple cyanobacterial genera, including Anabaena, Microcystis, and others.
- Putative interaction partners for these cyanobacterial calpains were predicted through in silico analysis.
- Phylogenetic analysis revealed two distinct monophyletic clusters for bacterial and eukaryotic calpains.
Conclusions:
- The study confirms the presence of calpains in diverse cyanobacteria, expanding their known bacterial distribution.
- Phylogenetic data support two evolutionary scenarios: acquisition by eukaryotes from bacteria or ancient inheritance from a common ancestor with subsequent losses.
- Both scenarios necessitate multiple independent gene losses in various bacterial and eukaryotic lineages.
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