ATP2/YJR121W Summary Help

ATP2 BASIC INFORMATION

Standard Name ATP2
Systematic Name YJR121W
Feature Type ORF, Verified
Description Beta subunit of the F1 sector of mitochondrial F1F0 ATP synthase, which is a large, evolutionarily conserved enzyme complex required for ATP synthesis; phosphorylated (1, 2 and see Summary Paragraph)
Name Description ATP synthase
GO Annotations All ATP2 GO evidence and references
    View Computational GO annotations for ATP2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Mutant Phenotype All ATP2 Phenotype details and references
Classical genetics
null
unspecified
Large-scale survey
null
Interactions ATP2 All interactions details and references
59 total interaction(s) for 32 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 16
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 2
  • Co-fractionation: 1
  • Co-purification: 34
  • Two-hybrid: 2
Genetic Interactions
  • Dosage Rescue: 1
  • Synthetic Growth Defect: 1
  • Synthetic Rescue: 1
Sequence Information
ChrX:647597 to 649132 | ORF Map | GBrowse
Gbrowse
Last Update Coordinates: 2009-02-18 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1536 647597..649132 2009-02-18 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000003882

ATP2 RESOURCES

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SGD ORF map
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  • Localization Resources
  • Interactions
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  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for ATP2

SUMMARY PARAGRAPH for ATP2

ATP2 encodes the beta subunit of mitochondrial F1-ATP synthase complex (3). The F0F1-ATP synthase complex can synthesize and hydrolyze ATP using a transmembrane proton gradient (4). 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 (5). The catalytic core of the enzyme resides in the F1 component and consists of a hexamer of alternating alpha (Atp1p) and beta subunits (6, 7). These three alpha-beta dimers each provide one of ATP synthase's three catalytic sites. Although isolated beta subunits are capable of binding nucleotide, both alpha and beta subunits are thought to contribute to nucleotide binding and catalysis (4).

Although ATP2 is essential for ATP synthase function, it is not essential for life in yeast. Deletion of ATP2, like deletions in many genes necessary for the function or maintenance of mitochondria, lead to a "petite" phenotype that is slow-growing and unable to survive on nonfermentable carbon sources (3). The 3' untranslated region of the ATP2 mRNA contains a sequence element that mediates localization of the mRNA to mitochondria; mutation of this element also results in a growth defect on nonfermentable carbon sources (8).

General ATP synthase structure and function are reviewed in references 4 and 9. For a review that is specific to yeast, see reference 5.

Last updated: 2007-10-23

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for ATP2]

1) Takeda M, et al.  (1985) Nuclear genes coding the yeast mitochondrial adenosine triphosphatase complex. Primary sequence analysis of ATP2 encoding the F1-ATPase beta-subunit precursor. J Biol Chem 260(29):15458-65
2) Reinders J, et al.  (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Mol Cell Proteomics 6(11):1896-906
3) Saltzgaber-Muller J, et al.  (1983) Nuclear genes coding the yeast mitochondrial adenosine triphosphatase complex. Isolation of ATP2 coding the F1-ATPase beta subunit. J Biol Chem 258(19):11465-70
4) Boyer PD  (1997) The ATP synthase--a splendid molecular machine. Annu Rev Biochem 66:717-49
5) 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
6) Abrahams JP, et al.  (1993) Inherent asymmetry of the structure of F1-ATPase from bovine heart mitochondria at 6.5 A resolution. EMBO J 12(5):1775-80
7) Abrahams JP, et al.  (1994) Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Nature 370(6491):621-8
8) Liu JM and Liu DR  (2007) Discovery of a mRNA mitochondrial localization element in Saccharomyces cerevisiae by nonhomologous random recombination and in vivo selection. Nucleic Acids Res 35(20):6750-61
9) Nakamoto RK, et al.  (1999) Rotational coupling in the F0F1 ATP synthase. Annu Rev Biophys Biomol Struct 28:205-34