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A novel Mitosomal β-barrel Outer Membrane Protein in Entamoeba.

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.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Santos HJ,Imai K,Makiuchi T,Tomii K,Horton P,Nozawa A,Ibrahim M,Tozawa Y,Nozaki T

doi

10.1038/srep08545

subject

Has Abstract

pub_date

2015-02-25 00:00:00

pages

8545

issn

2045-2322

pii

srep08545

journal_volume

5

pub_type

杂志文章

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