An ancestral bacterial division system is widespread in eukaryotic mitochondria
Open accessAbstract
Bacterial division initiates at the site of a contractile Z-ring composed of polymerized FtsZ. The location of the Z-ring in the cell is controlled by a system of three mutually antagonistic proteins, MinC, MinD, and MinE. Plastid division is also known to be dependent on homologs of these proteins, derived from the ancestral cyanobacterial endosymbiont that gave rise to plastids. In contrast, the mitochondria of model systems such as Saccharomyces cerevisiae , mammals, and Arabidopsis thaliana seem to have replaced the ancestral α-proteobacterial Min-based division machinery with host-derived dynamin-related proteins that form outer contractile rings. Here, we show that the mitochondrial division system of these model organisms is the exception, rather than the rule, for eukaryotes. We describe endosymbiont-derived, bacterial-like division systems comprising FtsZ and Min proteins in diverse less-studied eukaryote protistan lineages, including jakobid and heterolobosean excavates, a malawimonad, stramenopiles, amoebozoans, a breviate, and an apusomonad. For two of these taxa, the amoebozoan Dictyostelium purpureum and the jakobid Andalucia incarcerata , we confirm a mitochondrial localization of these proteins by their heterologous expression in Saccharomyces cerevisiae . The discovery of a proteobacterial-like division system in mitochondria of diverse eukaryotic lineages suggests that it was the ancestral feature of all eukaryotic mitochondria and has been supplanted by a host-derived system multiple times in distinct eukaryote lineages.
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Mammals lack a homolog of the fission protein FtsZ.
“However, mammals lack a homolog of the fission protein FtsZ [99].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [99]
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BindingDB Entry 50009901: Targeting the Bacterial Division Protein FtsZ.
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- Authors
- Leger, M. M., Petrů, M., Žárský, V., Eme, L., Vlček, Č., Harding, T., Lang, B. F., Eliáš, M., Doležal, P., & Roger, A. J.
- Affiliations
- Dalhousie University (CA)
- Charles University (CZ)
- Laboratory of Genomics and Bioinformatics, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, 142 20 Prague 4, Czech Republic;
- Université de Montréal (CA)
- University of Ostrava (CZ)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2015-03-23
- Volume
- 112
- Issue
- 33
- Pages
- 10239-10246
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC4547283
- OpenAlex
- W2163479977
- Cited by
- 76
- References
- 86
- Citations by year
- 2025: 4 · 2024: 6 · 2023: 4 · 2022: 5 · 2021: 10 · 2020: 9 · 2019: 5 · 2018: 6 · 2017: 14 · 2016: 12 · 2015: 1
- FWCI
- 4.77
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- ASEP (submittedVersion, public-domain)
- Funders
- Gouvernement du Canada | Canadian Institutes of Health Research (FRN#62809)
- Nova Scotia Health Research Foundation (CIHR-NSHRF Regional Partnership Program-Nova Scotia: RNS-62809, MED-ResearchPrograms-2012-8781)
- Gouvernement du Canada | Natural Sciences and Engineering Research Council of Canada (RGPIN 227085)
- Fonds National de la Recherche Luxembourg (PHD-08-001)
- Czech Science Foundation (13-24983S, 13-29423S)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protist diversity and phylogeny
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- mitochondrial division, FtsZ, Min proteins, MinC, mind, mines, endosymbiotic origin of mitochondria, cyanobacterial endosymbiont, Amoebozoa, Dictyostelium purpureum, dynamin-related proteins, mitochondrial localization, eukaryotic evolution
- MeSH terms
- Adenosine Triphosphatases, Bacteria, Bacterial Proteins, Base Sequence, Cell Division, Cytoskeletal Proteins, Dictyostelium, DNA, Bacterial, Mitochondria, Molecular Sequence Data, Phylogeny, Saccharomyces cerevisiae, Likelihood Functions, Arabidopsis, Plastids, Cell Cycle Proteins, Evolution, Molecular, Escherichia coli Proteins, Databases, Genetic, Mitochondrial Dynamics
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