Effects of VDAC isoforms on CuZn-superoxide dismutase activity in the intermembrane space of Saccharomyces cerevisiae mitochondria
| Autor: | Malgorzata Budzinska, Małgorzata Wojtkowska, Olgierd Stobienia, Hanna Galganska, Hanna Kmita |
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| Rok vydání: | 2007 |
| Předmět: |
Gene isoform
Voltage-dependent anion channel biology Superoxide Dismutase Cell Cycle Saccharomyces cerevisiae Biophysics Cell Biology Mitochondrion biology.organism_classification Biochemistry Enzyme Activation Superoxide dismutase Structure-Activity Relationship Cytosol Mitochondrial Membranes biology.protein Protein Isoforms Voltage-Dependent Anion Channels Intermembrane space Bacterial outer membrane Molecular Biology |
| Zdroj: | Biochemical and Biophysical Research Communications. 357:1065-1070 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2007.04.090 |
| Popis: | Copper and zinc containing superoxide dismutase (CuZnSOD) is located primarily in the cytosol but a small amount of the enzyme has also been identified in the intermembrane space of mitochondria (termed here IMS CuZnSOD). Using Saccharomyces cerevisiae mutants depleted of either isoform of VDAC (voltage-dependent anion-selective channel), we have shown that the activity of IMS CuZnSOD coincides with the presence of a given VDAC isoform and changes in a growth phase dependent way. Moreover, the IMS CuZnSOD activity correlates with the levels of O 2 - release from mitochondria and the cytosol redox state. The latter in turn seems to influence the levels of the mitochondrial outer membrane channel protein other than VDAC. Thus, we conclude that in the case of S. cerevisiae both VDAC isoforms influence the IMS CuZnSOD activity and subsequently the expression levels of some mitochondrial proteins. |
| Databáze: | OpenAIRE |
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