Linked Life Data

9305897

Source:http://linkedlifedata.com/resource/pubmed/id/9305897

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
39
pubmed:dateCreated
1997-10-23
pubmed:databankReference
pubmed:abstractText
The proteolipids of the vacuolar-type H+-ATPase (V-ATPase) are major components of the integral membrane sector. The vha-1 and vha-2 (vacuolar-type H+-ATPase) genes in Caenorhabditis elegans encode putative 16-kDa proteolipids and are tandemly localized on chromosome III. The vha-2 gene has three exons, whereas vha-1 has no introns. The deduced amino acid sequences of the two genes exhibit about 60% identity with the homologues from yeast, mouse, and cow. The mRNAs of both vha genes are trans-spliced to spliced leaders, suggesting that these genes constitute a polycistronic transcriptional unit. The vha-4 gene consists of four exons and is very similar to the yeast VMA16 gene that codes for the 23-kDa proteolipid. This is the first example of three distinct V-ATPase proteolipids being identified in higher eukaryotes. Northern blot and transgenic analyses show that the three vha genes may be highly expressed in the H-shaped excretory cell, rectum, and a pair of cells posterior to the anus. These results suggest that the V-ATPase activity may be important for exporting toxic compounds or metabolic wastes in this organism.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
24387-92
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Three vha genes encode proteolipids of Caenorhabditis elegans vacuolar-type ATPase. Gene structures and preferential expression in an H-shaped excretory cell and rectal cells.
pubmed:affiliation
Department of Molecular Cell Biology, Division of Biological Science, Institute of Scientific and Industrial Research, Osaka University, Osaka 567, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't