An ancestral bacterial division system is widespread in eukaryotic mitochondria
Identifieur interne : 000616 ( Ncbi/Curation ); précédent : 000615; suivant : 000617An ancestral bacterial division system is widespread in eukaryotic mitochondria
Auteurs : Michelle M. Leger ; Markéta Petrů [République tchèque] ; Vojt Ch Žársk [République tchèque] ; Laura Eme ; Estmír Vl Ek [République tchèque] ; Tommy Harding ; B. Franz Lang ; Marek Eliáš [République tchèque] ; Pavel Doležal [République tchèque] ; Andrew J. RogerSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2015.
Abstract
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
Url:
DOI: 10.1073/pnas.1421392112
PubMed: 25831547
PubMed Central: 4547283
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Michelle M. Leger<affiliation><nlm:aff id="aff1">Centre for Comparative Genomics and Evolutionary Bioinformatics (CGEB), Department of Biochemistry and Molecular Biology,<institution>Dalhousie University</institution>
, Halifax, NS,<country>Canada</country>
, B3H 4R2;</nlm:aff>
<wicri:noCountry code="subfield">B3H 4R2</wicri:noCountry>
</affiliation>
<affiliation><nlm:aff id="aff1">Centre for Comparative Genomics and Evolutionary Bioinformatics (CGEB), Department of Biochemistry and Molecular Biology,<institution>Dalhousie University</institution>
, Halifax, NS,<country>Canada</country>
, B3H 4R2;</nlm:aff>
<wicri:noCountry code="subfield">B3H 4R2</wicri:noCountry>
</affiliation>
<affiliation><nlm:aff id="aff1">Centre for Comparative Genomics and Evolutionary Bioinformatics (CGEB), Department of Biochemistry and Molecular Biology,<institution>Dalhousie University</institution>
, Halifax, NS,<country>Canada</country>
, B3H 4R2;</nlm:aff>
<wicri:noCountry code="subfield">B3H 4R2</wicri:noCountry>
</affiliation>
<affiliation><nlm:aff wicri:cut="; and" id="aff4">Robert Cedergren Centre for Bioinformatics and Genomics, Département de Biochimie,<institution>Université de Montréal</institution>
, Montreal, QC,<country>Canada</country>
, H3T 1J4</nlm:aff>
<wicri:noCountry code="subfield">H3T 1J4</wicri:noCountry>
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, Halifax, NS,<country>Canada</country>
, B3H 4R2;</nlm:aff>
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<front><div type="abstract" xml:lang="en"><p>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 <italic>Saccharomyces cerevisiae</italic>
, mammals, and <italic>Arabidopsis thaliana</italic>
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 <italic>Dictyostelium purpureum</italic>
and the jakobid <italic>Andalucia incarcerata</italic>
, we confirm a mitochondrial localization of these proteins by their heterologous expression in <italic>Saccharomyces cerevisiae</italic>
. 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.</p>
</div>
</front>
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