Ferens 2017 Biochem Cell Biol: Difference between revisions
(Created page with "{{Publication |title=Ferens FG, Spicer V, Krokhin OV, Motnenko A, Summers WA, Court DA (2017) A deletion variant partially complements a porin-less strain of ''Neurospora cras...") Β |
No edit summary Β |
||
| Line 6: | Line 6: | ||
|journal=Biochem Cell Biol | |journal=Biochem Cell Biol | ||
|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 (ΞPor-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 ΞPor-1 strain. These, and other proteins related to electron flow and mitochondrial biogenesis, are differentially affected by relative porin levels. | |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 (ΞPor-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 ΞPor-1 strain. These, and other proteins related to electron flow and mitochondrial biogenesis, are differentially affected by relative porin levels. | ||
|keywords=Alternative oxidase | |||
|editor=[[Kandolf G]], | |editor=[[Kandolf G]], | ||
}} | }} | ||
| Line 14: | Line 15: | ||
|enzymes=Complex I, Complex III, Complex IV;cytochrome c oxidase | |enzymes=Complex I, Complex III, Complex IV;cytochrome c oxidase | ||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
|additional= | |additional=2017-07, | ||
}} | }} | ||
Latest revision as of 13:18, 25 June 2019
| 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. |
Ferens FG, Spicer V, Krokhin OV, Motnenko A, Summers WA, Court DA (2017) Biochem Cell Biol
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 (ΞPor-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 ΞPor-1 strain. These, and other proteins related to electron flow and mitochondrial biogenesis, are differentially affected by relative porin levels. β’ Keywords: Alternative oxidase β’ Bioblast editor: Kandolf G
Labels: MiParea: Respiration, mt-Biogenesis;mt-density
Organism: Fungi
Preparation: Isolated mitochondria Enzyme: Complex I, Complex III, Complex IV;cytochrome c oxidase
HRR: Oxygraph-2k
2017-07
