Ferens 2017 Biochem Cell Biol
|Ferens FG, Spicer V, Krokhin OV, Motnenko A, Summers WA, Court DA (2017) A deletion variant partially complements a porin-less strain of Neurospora crassa. Biochem Cell Biol 95:318-27.|
Abstract: Mitochondrial porin, the voltage-dependent anion channel, plays an important role in metabolism and other cellular functions within eukaryotic cells. To further the understanding of porin structure and function, Neurospora crassa wild-type porin was replaced with a deletion variant lacking residues 238-242 (238porin). 238porin was assembled in the mitochondrial outer membrane, but the steady state levels were only about 3% of those of the wild-type protein. The strain harbouring 238porin displayed cytochrome deficiencies and expressed alternative oxidase. Nonetheless, it exhibited an almost normal linear growth rate. Analysis of mitochondrial proteomes from a wild-type strain FGSC9718, a strain lacking porin (ΔPor-1), and one expressing only 238porin, revealed that the major differences between the variant strains were in the levels of subunits of the NADH:ubiquinone oxidoreductase (complex I) of the electron transport chain, which were reduced only in the ΔPor-1 strain. These, and other proteins related to electron flow and mitochondrial biogenesis, are differentially affected by relative porin levels.
• Bioblast editor: Kandolf G
Labels: MiParea: Respiration, mt-Biogenesis;mt-density
Preparation: Isolated mitochondria Enzyme: Complex I, Complex III, Complex IV;cytochrome c oxidase