Molecular cloning and characterization of a novel form of the human vacuolar H +-ATPase e-subunit: An essential proton pump component

Several of the 13 subunits comprising mammalian H +-ATPases have multiple alternative forms, encoded by separate genes and with differing tissue expression patterns. These may play an important role in the intracellular localization and activity of H +-ATPases. Here we report the cloning of a previo...

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Bibliographic Details
Published in:Gene 2007-05, Vol.393 (1), p.94-100
Main Authors: Blake-Palmer, Katherine G., Su, Ya, Smith, Annabel N., Karet, Fiona E.
Format: Article
Language:English
Subjects:
Acidosis, Renal Tubular - enzymology
Acidosis, Renal Tubular - genetics
Alternative Splicing - genetics
Amino Acid Sequence
Brain
Cloning, Molecular
DNA, Complementary - genetics
Gene Expression Profiling
Gene Expression Regulation
Genetic Complementation Test
H +-ATPase
Humans
Kidney
Molecular Sequence Data
Protein Subunits - chemistry
Protein Subunits - genetics
Protein Subunits - metabolism
Proton pump
Proton Pumps - genetics
RNA, Messenger - genetics
RNA, Messenger - metabolism
Subunit
Vacuolar Proton-Translocating ATPases - chemistry
Vacuolar Proton-Translocating ATPases - genetics
Vacuolar Proton-Translocating ATPases - metabolism
Yeasts - growth & development
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Summary:Several of the 13 subunits comprising mammalian H +-ATPases have multiple alternative forms, encoded by separate genes and with differing tissue expression patterns. These may play an important role in the intracellular localization and activity of H +-ATPases. Here we report the cloning of a previously uncharacterized human gene, ATP6V0E2, encoding a novel H +-ATPase e-subunit designated e2. We demonstrate that in contrast to the ubiquitously expressed gene encoding the e1 subunit (previously called e), this novel gene is expressed in a more restricted tissue distribution, particularly kidney and brain. We show by complementation studies in a yeast strain deficient for the ortholog of this subunit, that either form of the e-subunit is essential for proper proton pump function. The identification of this novel form of the e-subunit lends further support to the hypothesis that subunit differences may play a key role in the structure, site and function of H +-ATPases within the cell.
ISSN:0378-1119
1879-0038
DOI:10.1016/j.gene.2007.01.020