| http://purl.uniprot.org/citations/17897940 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17897940 | http://www.w3.org/2000/01/rdf-schema#comment | "The vacuolar ATPases (V-ATPases) are multisubunit complexes containing two domains. The V(1) domain (subunits A-H) is peripheral and carries out ATP hydrolysis. The V(0) domain (subunits a, c, c', c'', d, and e) is membrane-integral and carries out proton transport. In yeast, there are three proteolipid subunits as follows: subunit c (Vma3p), subunit c' (Vma11p), and subunit c'' (Vma16p). The proteolipid subunits form a six-membered ring containing single copies of subunits c' and c'' and four copies of subunit c. To determine the possible arrangements of proteolipid subunits in V(0) that give rise to a functional V-ATPase complex, a series of gene fusions was constructed to constrain the arrangement of pairs of subunits in the ring. Fusions containing c'' employed a truncated version of this protein lacking the first putative transmembrane helix (which we have shown previously to be functional), to ensure that the N and C termini of all subunits were located on the luminal side of the membrane. Fusion constructs were expressed in strains disrupted in c', c'', or both but containing a wild copy of c to ensure the presence of the required number of copies of subunit c. The c-c''(DeltaTM1), c''(DeltaTM1)-c', and c'-c constructs all complemented the vma(-) phenotype and gave rise to complexes possessing greater than 25% of wild-type levels of activity. By contrast, neither the c-c', the c'-c''(DeltaTM1), nor the c''(DeltaTM1)-c constructs complemented the vma(-) phenotype. These results suggest that functionally assembled V-ATPase complexes contain the proteolipid subunits arranged in a unique order in the ring."xsd:string |
| http://purl.uniprot.org/citations/17897940 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m704331200"xsd:string |
| http://purl.uniprot.org/citations/17897940 | http://purl.uniprot.org/core/author | "Wang Y."xsd:string |
| http://purl.uniprot.org/citations/17897940 | http://purl.uniprot.org/core/author | "Forgac M."xsd:string |
| http://purl.uniprot.org/citations/17897940 | http://purl.uniprot.org/core/author | "Cipriano D.J."xsd:string |
| http://purl.uniprot.org/citations/17897940 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17897940 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/17897940 | http://purl.uniprot.org/core/pages | "34058-34065"xsd:string |
| http://purl.uniprot.org/citations/17897940 | http://purl.uniprot.org/core/title | "Arrangement of subunits in the proteolipid ring of the V-ATPase."xsd:string |
| http://purl.uniprot.org/citations/17897940 | http://purl.uniprot.org/core/volume | "282"xsd:string |
| http://purl.uniprot.org/citations/17897940 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17897940 |
| http://purl.uniprot.org/citations/17897940 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17897940 |
| http://purl.uniprot.org/uniprot/#_P23968-mappedCitation-17897940 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17897940 |
| http://purl.uniprot.org/uniprot/#_P25515-mappedCitation-17897940 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17897940 |
| http://purl.uniprot.org/uniprot/#_P32842-mappedCitation-17897940 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17897940 |
| http://purl.uniprot.org/uniprot/P25515 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/17897940 |
| http://purl.uniprot.org/uniprot/P32842 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/17897940 |
| http://purl.uniprot.org/uniprot/P23968 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/17897940 |