| Autor: |
Ferens FG; a Department of Microbiology, University of Manitoba, Winnipeg, MB R3T 2N2, Canada., Spicer V; b Department of Physics and Astronomy, University of Manitoba, Winnipeg, MB R3T 2N2, Canada., Krokhin OV; c Department of Internal Medicine & Manitoba Centre for Proteomics and Systems Biology, University of Manitoba, Winnipeg, MB R3E 3P4, Canada., Motnenko A; a Department of Microbiology, University of Manitoba, Winnipeg, MB R3T 2N2, Canada., Summers WA; a Department of Microbiology, University of Manitoba, Winnipeg, MB R3T 2N2, Canada., Court DA; a Department of Microbiology, University of Manitoba, Winnipeg, MB R3T 2N2, Canada. |
| Abstrakt: |
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. |
