Hetero-oligomer of dynamin-related proteins participates in the fission of highly divergent mitochondria from Entamoeba histolytica

Makiuchi, Takashi; Santos, Herbert J.; Tachibana, Hiroshi; Nozaki, Tomoyoshi

doi:10.1038/s41598-017-13721-5

Cited by 18 publications

(23 citation statements)

References 56 publications

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“…The homologous genes are also conserved in E. invadens (EIN_051430, EIN_070060 and EIN_254810) (Makiuchi et al. ), and the presence of these molecules and our observation suggest the possibility of dispersion of donor mitosome proteins.…”

Section: Discussionsupporting

confidence: 70%

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Influence of Heterologous Transplant of DNA‐lacking Mitochondria from Entamoeba histolytica on Proliferation of Entamoeba invadens

Kazama

Yoshida

Ogiwara

et al. 2018

J Eukaryotic Microbiology

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In mitochondria, compatibility of proteins encoded in mitochondrial DNA and nuclear DNA is essential for the normal functioning of the organelle. Incompatibility between mitochondrial and nuclear DNA can lead to dysfunctional respiration, mitochondrial diseases, and lethal problems, which suggests that the presence of heterologous mitochondria is unfavorable. In a previous study, we established a transplant method for DNA‐lacking mitochondria (mitosomes) in the anaerobic protozoan Entamoeba histolytica. In this study, interspecies transplant of mitosomes from E. histolytica into Entamoeba invadens, which is a parasitic protozoon of reptiles, was performed using the microinjection method at various temperatures and injection volumes. When E. invadens was used as recipient, it showed higher tolerance to a lower temperature and larger injection volume, in comparison with E. histolytica. After microinjection, donor mitosomes expressing HA‐tag conjugated protein were observed in recipient cells by immunofluorescent staining. The heterologous mitosomes‐injected cells proliferated and growth rate of the microinjected‐cells was similar to that of intact cells. Therefore, we conclude that interspecies transplant of DNA‐lacking mitochondria does not result in incompatibility.

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Section: Discussionsupporting

confidence: 70%

“…Mitosomal fission in E. histolytica is associated with dynamin‐related proteins that are also involved in mitochondrial fission (Makiuchi et al. ). The homologous genes are also conserved in E. invadens (EIN_051430, EIN_070060 and EIN_254810) (Makiuchi et al.…”

Section: Discussionmentioning

confidence: 99%

Influence of Heterologous Transplant of DNA‐lacking Mitochondria from Entamoeba histolytica on Proliferation of Entamoeba invadens

Kazama

Yoshida

Ogiwara

et al. 2018

J Eukaryotic Microbiology

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“…All these results strongly suggest that the hetero-oligomerization is required for these molecules to accumulate at the cleavage furrow. The hetero-oligomerization of dynamins has been recently identified in mitochondrion fission in Entamoeba histolytica [41].…”

Section: Discussionmentioning

confidence: 99%

Dynamin-Like Protein B of Dictyostelium Contributes to Cytokinesis Cooperatively with Other Dynamins

Fujimoto

Tanaka

Rana

et al. 2019

Cells

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Dynamin is a large GTPase responsible for diverse cellular processes, such as endocytosis, division of organelles, and cytokinesis. The social amoebozoan, Dictyostelium discoideum, has five dynamin-like proteins: dymA, dymB, dlpA, dlpB, and dlpC. DymA, dlpA, or dlpB-deficient cells exhibited defects in cytokinesis. DlpA and dlpB were found to colocalize at cleavage furrows from the early phase, and dymA localized at the intercellular bridge connecting the two daughter cells, indicating that these dynamins contribute to cytokinesis at distinct dividing stages. Total internal reflection fluorescence microscopy revealed that dlpA and dlpB colocalized at individual dots at the furrow cortex. However, dlpA and dlpB did not colocalize with clathrin, suggesting that they are not involved in clathrin-mediated endocytosis. The fact that dlpA did not localize at the furrow in dlpB null cells and vice versa, as well as other several lines of evidence, suggests that hetero-oligomerization of dlpA and dlpB is required for them to bind to the furrow. The hetero-oligomers directly or indirectly associate with actin filaments, stabilizing them in the contractile rings. Interestingly, dlpA, but not dlpB, accumulated at the phagocytic cups independently of dlpB. Our results suggest that the hetero-oligomers of dlpA and dlpB contribute to cytokinesis cooperatively with dymA.

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“…We also noticed slight elongation of mitosomes stained by anti-APSK antiserum in the ETMP30gs strain (Figure 4d). However, this phenotype was not as severe as the morphological defects observed in DrpA and DrpB gene silenced strains and the strains expressing dominant negative DrpA or DrpB mutant reported previously [31].…”

Section: Resultsmentioning

confidence: 44%

An Entamoeba-Specific Mitosomal Membrane Protein with Potential Association to the Golgi Apparatus

Santos

Hanadate

Imai

et al. 2019

Genes

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The aerobic mitochondrion had undergone evolutionary diversification, most notable among lineages of anaerobic protists. Entamoeba is one of the genera of parasitic protozoans that lack canonical mitochondria, and instead possess mitochondrion-related organelles (MROs), specifically mitosomes. Entamoeba mitosomes exhibit functional reduction and divergence, most exemplified by the organelle’s inability to produce ATP and synthesize iron-sulfur cluster. Instead, this organelle is capable of sulfate activation, which has been linked to amoebic stage conversion. In order to understand other unique features and components of this MRO, we utilized an in silico prediction tool to screen transmembrane domain containing proteins in the mitosome proteome. Here, we characterize a novel lineage-specific mitosomal membrane protein, named Entamoeba transmembrane mitosomal protein of 30 kDa (ETMP30; EHI_172170), predicted to contain five transmembrane domains. Immunofluorescence analysis demonstrated colocalization of hemagglutinin (HA)-tagged ETMP30 with the mitosomal marker, adenosine-5’-phosphosulfate kinase. Mitosomal membrane localization was indicated by immunoelectron microscopy analysis, which was supported by carbonate fractionation assay. Transcriptional gene silencing successfully repressed RNA expression by 60%, and led to a defect in growth and partial elongation of mitosomes. Immunoprecipitation of ETMP30 from ETMP30-HA-expressing transformant using anti-HA antibody pulled down one interacting protein of 126 kDa. Protein sequencing by mass spectrometry revealed this protein as a cation-transporting P-type ATPase, previously reported to localize to vacuolar compartments/Golgi-like structures, hinting at a possible mitosome-vacuole/Golgi contact site.

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Hetero-oligomer of dynamin-related proteins participates in the fission of highly divergent mitochondria from Entamoeba histolytica

Cited by 18 publications

References 56 publications

Influence of Heterologous Transplant of DNA‐lacking Mitochondria from Entamoeba histolytica on Proliferation of Entamoeba invadens

Influence of Heterologous Transplant of DNA‐lacking Mitochondria from Entamoeba histolytica on Proliferation of Entamoeba invadens

Dynamin-Like Protein B of Dictyostelium Contributes to Cytokinesis Cooperatively with Other Dynamins

An Entamoeba-Specific Mitosomal Membrane Protein with Potential Association to the Golgi Apparatus

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