| Standard Name | OLI1 1 (see Nomenclature conflict Note) |
|---|---|
| Systematic Name | Q0130 |
| Alias | ATP9 , OLI3 2 |
| Feature Type | ORF, Verified |
| Description | F0-ATP synthase subunit c (ATPase-associated proteolipid), encoded on the mitochondrial genome; mutation confers oligomycin resistance; expression is specifically dependent on the nuclear genes AEP1 and AEP2 (1, 3, 4, 5 and see Summary Paragraph) |
| Name Description | OLIgomycin resistance 1 |
| Chromosomal Location | |
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| View Computational GO annotations for OLI1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
| Classical genetics | |
|---|---|
| conditional | |
| reduction of function |
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| Resources |
| 16 total interaction(s) for 10 unique genes/features. | |
| Physical Interactions |
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| Resources |
| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
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| Last Update | Coordinates: 2000-05-19 | Sequence: 2000-05-19 | ||||||||||||
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| S288C only | |
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| S288C vs. other species | |
| S288C vs. other strains |
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000007274 |
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NOMENCLATURE CONFLICT NOTE
| Name | Relevance | Description |
|---|---|---|
| PHO2 | Nomenclature conflict | PHO2 has been used to refer to both PHO2/YDL106C, which encodes a transcription factor, and OLI1/Q0130, the mitochondrial gene encoding an ATP synthase subunit. |
| PDR1 | Nomenclature conflict | OLI1 has been used to refer to both OLI1/Q0130, the mitochondrial gene encoding an ATP synthase subunit, and PDR1/YGL013C, which encodes a transcription factor. |
OLI1 is one of three mitochondrial genes, along with ATP8 and ATP6, that encode ATP synthase subunits. Also known as subunit 9 or Y9, Oli1p is homologous to subunit c of bacterial ATP synthase (6 and references therein). The ATP synthase complex utilizes proton motive force to generate ATP from ADP and Pi (7). The structure of this enzyme complex is highly conserved among diverse organisms and consists of two major components, soluble F1 and membrane-bound F0, each of which contains many subunits. The F0 proton pore is formed by a ring of twelve Y9 subunits. It is hypothesized that ATP synthase activity is driven by the rotation of the Y9 ring and subsequent transfer of that rotational force to the F1 catalytic core (7 and 8).
Although OLI1 is essential for ATP synthase function, it is not essential for life in yeast. Deletion of OLI1, like deletions in many genes necessary for the function or maintenance of mitochondria, leads to a "petite" phenotype that is slow-growing and unable to survive on nonfermentable carbon sources (9).
General ATP synthase structure and function are reviewed in references 7 and 8. For a review that is specific to yeast, see reference 6.
| 1) | Trembath MK, et al. (1975) Biogenesis of mitochondria 36, The genetic and biochemical analysis of a mitochondrially determined cold sensitive oligomycin resistant mutant of Saccharomyces cerevisiae with affected mitochondrial ATPase assembly. Mol Gen Genet 141(1):9-22 |
| 2) | Ooi BG, et al. (1985) DNA sequence analysis of the oli1 gene reveals amino acid changes in mitochondrial ATPase subunit 9 from oligomycin-resistant mutants of Saccharomyces cerevisiae. Eur J Biochem 152(3):709-14 |
| 3) | Nagley P, et al. (1986) Amino acid substitutions in mitochondrial ATPase subunit 9 of Saccharomyces cerevisiae leading to oligomycin or venturicidin resistance. FEBS Lett 195(1-2):159-63 |
| 4) | Payne MJ, et al. (1993) Characterization of a second nuclear gene, AEP1, required for expression of the mitochondrial OLI1 gene in Saccharomyces cerevisiae. Curr Genet 24(1-2):126-35 |
| 5) | Finnegan PM, et al. (1991) Characterization of a yeast nuclear gene, AEP2, required for accumulation of mitochondrial mRNA encoding subunit 9 of the ATP synthase. Curr Genet 20(1-2):53-61 |
| 6) | Devenish RJ, et al. (2000) Insights into ATP synthase assembly and function through the molecular genetic manipulation of subunits of the yeast mitochondrial enzyme complex. Biochim Biophys Acta 1458(2-3):428-42 |
| 7) | Boyer PD (1997) The ATP synthase--a splendid molecular machine. Annu Rev Biochem 66:717-49 |
| 8) | Nakamoto RK, et al. (1999) Rotational coupling in the F0F1 ATP synthase. Annu Rev Biophys Biomol Struct 28:205-34 |
| 9) | Somlo M, et al. (1977) An oligomycin-resistant adenosine triphosphatase and its effects on cellular growth, mitochondrial oxidative phosphorylation and respiratory proton translocation in Saccharomyces cerevisiae. Biochem J 162(1):51-9 |





