ATP6/Q0085 Summary Help

Standard Name ATP6
Systematic Name Q0085
Alias OLI2 , OLI4 , PHO1
Feature Type ORF, Verified
Description Subunit a of the F0 sector of mitochondrial F1F0 ATP synthase; mitochondrially encoded; translation is specifically activated by Atp22p; ATP6 and ATP8 mRNAs are not translated in the absence of the F1 sector of ATPase (1, 2, 3 and see Summary Paragraph)
Name Description ATP synthase
Chromosomal Location
ChrMito:28487 to 29266 | ORF Map | GBrowse
Gene Ontology Annotations All ATP6 GO evidence and references
  View Computational GO annotations for ATP6
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Classical genetics
reduction of function
36 total interaction(s) for 20 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 16
  • Affinity Capture-Western: 10
  • Co-fractionation: 1
  • Co-purification: 4
  • Reconstituted Complex: 2
  • Two-hybrid: 1

Genetic Interactions
  • Phenotypic Suppression: 1
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 259
Molecular Weight (Da) 29,099
Isoelectric Point (pI) 8.42
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrMito:28487 to 29266 | ORF Map | GBrowse
Last Update Coordinates: 2000-05-19 | Sequence: 2000-05-19
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..780 28487..29266 2000-05-19 2000-05-19
Retrieve sequences
Analyze Sequence
S288C only
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
Primary SGDIDS000007268

ATP6 is one of three mitochondrial genes, along with ATP8 and OLI1, that encode ATP synthase subunits. Also known as subunit 6 or Y6, Atp6p is homologous to subunit a of bacterial ATP synthase (4 and references therein). The ATP synthase complex utilizes proton motive force to generate ATP from ADP and Pi (5). 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. Y6 is a component of F0. It is hypothesized that Y6, an integral membrane protein, provides a stationary structure necessary for the productive rotation of Y9 (Oli1p) subunits and the resulting coupling of proton motive force to ATP synthesis.(5, 6).

Although ATP6 is essential for ATP synthase function, it is not essential for life in yeast. Deletion of ATP6, 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 (7).

General ATP synthase structure and function are reviewed in references 5 and 6. For a review that is specific to yeast, see reference 4.

Last updated: 2006-04-03 Contact SGD

References cited on this page View Complete Literature Guide for ATP6
1) John UP and Nagley P  (1986) Amino acid substitutions in mitochondrial ATPase subunit 6 of Saccharomyces cerevisiae leading to oligomycin resistance. FEBS Lett 207(1):79-83
2) Zeng X, et al.  (2007) The Saccharomyces cerevisiae ATP22 gene codes for the mitochondrial ATPase subunit 6-specific translation factor. Genetics 175(1):55-63
3) Rak M and Tzagoloff A  (2009) F1-dependent translation of mitochondrially encoded Atp6p and Atp8p subunits of yeast ATP synthase. Proc Natl Acad Sci U S A 106(44):18509-14
4) 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
5) Boyer PD  (1997) The ATP synthase--a splendid molecular machine. Annu Rev Biochem 66:717-49
6) Nakamoto RK, et al.  (1999) Rotational coupling in the F0F1 ATP synthase. Annu Rev Biophys Biomol Struct 28():205-34
7) Roberts H, et al.  (1979) mit- Mutations in the oli2 region of mitochondrial DNA affecting the 20 000 dalton subunit of the mitochondrial ATPase in Saccharomyces cerevisiae. FEBS Lett 108(2):501-4