ArticleScientific reports2015
A novel Mitosomal β-barrel Outer Membrane Protein in Entamoeba.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Evolution and Adaptation of the Mitochondrial Protein Import Machinery in Parasitic Protists: Beyond the Canonical TOM Complex.International journal of molecular sciences · 2026Review
- An atypical venus fly trap domain receptor regulates motility and phagocytosis in the protozoan parasite Entamoeba histolytica.PLoS pathogens · 2026Article
- The mitosome of the anaerobic parasitic protist Entamoeba histolytica: A peculiar and minimalist mitochondrion-related organelle.The Journal of eukaryotic microbiology · 2022Review
- Article
- Import ofMicroorganisms · 2020Article
- Dynamism of PI4-Phosphate during Interactions with Human Erythrocytes inMicroorganisms · 2020Article
- Article
- AnGenes · 2019Article
- Spectroscopic analysis of chlamydial major outer membrane protein in support of structure elucidation.Protein science : a publication of the Protein Society · 2018Article
- Properties of Omp2a-Based Supported Lipid Bilayers: Comparison with Polymeric Bioinspired Membranes.ACS omega · 2018Article
- The emerging picture of the mitochondrial protein import complexes of Amoebozoa supergroup.BMC genomics · 2017Article
- Hetero-oligomer of dynamin-related proteins participates in the fission of highly divergent mitochondria from Entamoeba histolytica.Scientific reports · 2017Article
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9 authors.
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Abstract
Entamoeba possesses a highly divergent mitochondrion-related organelle known as the mitosome. Here, we report the discovery of a novel protein in Entamoeba, which we name Mitosomal β-barrel Outer Membrane Protein of 30 kDa (MBOMP30). Initially identified through in silico analysis, we experimentally confirmed that MBOMP30 is indeed a β-barrel protein. Circular dichroism analysis showed MBOMP30 has a predominant β-sheet structure. Localization to Entamoeba histolytica mitosomes was observed through Percoll-gradient fractionation and immunofluorescence assay. Mitosomal membrane integration was demonstrated by carbonate fractionation, proteinase K digestion, and immunoelectron microscopy. Interestingly, the deletion of the putative β-signal, a sequence believed to guide β-barrel outer membrane protein (BOMP) assembly, did not affect membrane integration, but abolished the formation of a ~240 kDa complex. MBOMP30 represents only the seventh subclass of eukaryotic BOMPs discovered to date and lacks detectable homologs outside Entamoeba, suggesting that it may be unique to Entamoeba mitosomes.
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