Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2003-1-15
pubmed:databankReference
pubmed:abstractText
Vacuolar-type proton-translocating ATPases (V-ATPases), multimeric proton pumps, are involved in a wide variety of physiological processes. For their diverse functions, V-ATPases utilize a specific subunit isoform(s). Here, we reported the molecular cloning and characterization of three novel subunit isoforms, C2, d2 and G3, of mouse V-ATPase. These isoforms were expressed in a tissue-specific manner, in contrast to the ubiquitously expressed C1, d1 and G1 isoforms. C2 was expressed predominantly in lung and kidney, and d2 and G3 specifically in kidney. We introduced these isoforms into yeasts lacking the corresponding genes. Although the G3 and d2 did not rescue the vmaDelta phenotype, d1 and the two C isoforms functionally complemented the Deltavma6 and Deltavma5, respectively, indicating that they are bona fide subunits of V-ATPase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
302
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
147-53
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:12527205-Amino Acid Sequence, pubmed-meshheading:12527205-Animals, pubmed-meshheading:12527205-Blotting, Northern, pubmed-meshheading:12527205-Cloning, Molecular, pubmed-meshheading:12527205-DNA, Complementary, pubmed-meshheading:12527205-Gene Expression Regulation, Enzymologic, pubmed-meshheading:12527205-Genetic Complementation Test, pubmed-meshheading:12527205-Genetic Variation, pubmed-meshheading:12527205-Male, pubmed-meshheading:12527205-Mice, pubmed-meshheading:12527205-Molecular Sequence Data, pubmed-meshheading:12527205-Mutation, pubmed-meshheading:12527205-Protein Isoforms, pubmed-meshheading:12527205-Protein Subunits, pubmed-meshheading:12527205-Proton Pumps, pubmed-meshheading:12527205-RNA, Messenger, pubmed-meshheading:12527205-Saccharomyces cerevisiae, pubmed-meshheading:12527205-Sequence Alignment, pubmed-meshheading:12527205-Sequence Analysis, DNA, pubmed-meshheading:12527205-Sequence Homology, Amino Acid, pubmed-meshheading:12527205-Vacuolar Proton-Translocating ATPases
pubmed:year
2003
pubmed:articleTitle
Diversity of mouse proton-translocating ATPase: presence of multiple isoforms of the C, d and G subunits.
pubmed:affiliation
Division of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University, and CREST (Core Research for Evolutional Science and Technology), Japan Science and Technology Corp., Mihogaoka 8-1, Ibaraki-shi, Osaka 567-0047, Japan.
pubmed:publicationType
Journal Article