rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
1
|
pubmed:dateCreated |
1996-11-7
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pubmed:databankReference |
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pubmed:abstractText |
Phosphatidylinositol synthase (CDP-1,2-diacyl-sn-glycerol: 3-phosphatidyltransferase, EC 2.7.8.11) catalyzes the formation of phosphatidylinositol and CMP from CDP-diacylglycerol and myo-inositol. We have cloned a phosphatidylinositol synthase cDNA from rat brain by functional complementation of the yeast pis mutation, which is defective in phosphatidylinositol synthase. The deduced protein comprised 213 amino acids with a calculated molecular mass of 23,613 Da. The predicted protein sequence is highly homologous to the previously determined yeast phosphatidylinositol synthase sequence. The cDNA hybridized to a 1.7-kb mRNA that was abundantly expressed in rat brain and kidney.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Sep
|
pubmed:issn |
0014-5793
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
9
|
pubmed:volume |
393
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
89-92
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8804431-Amino Acid Sequence,
pubmed-meshheading:8804431-Animals,
pubmed-meshheading:8804431-Base Sequence,
pubmed-meshheading:8804431-Brain,
pubmed-meshheading:8804431-CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase,
pubmed-meshheading:8804431-Cloning, Molecular,
pubmed-meshheading:8804431-DNA, Complementary,
pubmed-meshheading:8804431-Genetic Complementation Test,
pubmed-meshheading:8804431-Membrane Proteins,
pubmed-meshheading:8804431-Molecular Sequence Data,
pubmed-meshheading:8804431-Mutation,
pubmed-meshheading:8804431-RNA, Messenger,
pubmed-meshheading:8804431-Rats,
pubmed-meshheading:8804431-Saccharomyces cerevisiae,
pubmed-meshheading:8804431-Tissue Distribution,
pubmed-meshheading:8804431-Transferases (Other Substituted Phosphate Groups)
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pubmed:year |
1996
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pubmed:articleTitle |
Molecular cloning of rat phosphatidylinositol synthase cDNA by functional complementation of the yeast Saccharomyces cerevisiae pis mutation.
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pubmed:affiliation |
Department of Biochemistry, Gunma University School of Medicine, Maebashi, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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