ArticlePloS one2011
The Neurospora crassa TOB complex: analysis of the topology and function of Tob38 and Tob37.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed.
- Building Better Barrels - β-barrel Biogenesis and Insertion in Bacteria and Mitochondria.Journal of molecular biology · 2021Review
- Phosphatidylcholine affects the role of the sorting and assembly machinery in the biogenesis of mitochondrial β-barrel proteins.The Journal of biological chemistry · 2015Article
- Fitting the Pieces of the β-Barrel Assembly Machinery Complex.Biochemistry · 2015Review
- Sam37 is crucial for formation of the mitochondrial TOM-SAM supercomplex, thereby promoting β-barrel biogenesis.The Journal of cell biology · 2015Article
- Role of phosphatidylethanolamine in the biogenesis of mitochondrial outer membrane proteins.The Journal of biological chemistry · 2013Article
- Article
- Characterization of the insertase for β-barrel proteins of the outer mitochondrial membrane.The Journal of cell biology · 2012Article
- Dynamic association of BAM complex modules includes surface exposure of the lipoprotein BamC.Journal of molecular biology · 2012Article
- Mitochondrial sorting and assembly machinery subunit Sam37 in Candida albicans: insight into the roles of mitochondria in fitness, cell wall integrity, and virulence.Eukaryotic cell · 2012Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The TOB or SAM complex is responsible for assembling several proteins into the mitochondrial outer membrane, including all β-barrel proteins. We have identified several forms of the complex in Neurospora crassa. One form contains Tob55, Tob38, and Tob37; another contains these three subunits plus the Mdm10 protein; while additional complexes contain only Tob55. As previously shown for Tob55, both Tob37 and Tob38 are essential for viability of the organism. Mitochondria deficient in Tob37 or Tob38 have reduced ability to assemble β-barrel proteins. The function of two hydrophobic domains in the C-terminal region of the Tob37 protein was investigated. Mutant Tob37 proteins lacking either or both of these regions are able to restore viability to cells lacking the protein. One of the domains was found to anchor the protein to the outer mitochondrial membrane but was not necessary for targeting or association of the protein with mitochondria. Examination of the import properties of mitochondria containing Tob37 with deletions of the hydrophobic domains reveals that the topology of Tob37 may be important for interactions between specific classes of β-barrel precursors and the TOB complex.
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Registered trials
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