Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1993-3-3
pubmed:abstractText
The yeast vacuolar proton-translocating ATPase was discovered in 1981 as the first member of the V-ATPases, which are now known to be ubiquitously distributed in eukaryotic vacuo-lysosomal organelles and archaebacteria. Nine VMA genes that are indispensable for expression of vacuolar ATPase activity have been identified in the yeast Saccharomyces cerevisiae. VMA1, VMA2, VMA3, VMA5 and VMA6 were cloned and characterized on the basis of partial amino acid sequences determined with the purified subunits. Genetic and biochemical studies of the yeast Pet-cls mutants have demonstrated that they are related to vma defects. Based on this evidence, VMA11 (CLS9), VMA12 (CLS10) and VMA13 (CLS11) were isolated from a yeast genomic DNA library by complementation of the vma11, vma12 and vma13 mutations, respectively. This article summarizes currently available information on the VMA genes and the molecular biological functions of the VMA gene products.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-0949
pubmed:author
pubmed:issnType
Print
pubmed:volume
172
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
67-81
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Molecular genetics of the yeast vacuolar H(+)-ATPase.
pubmed:affiliation
Department of Biology, Faculty of Science, University of Tokyo, Japan.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't