Linked Life Data

9880566

Source:http://linkedlifedata.com/resource/pubmed/id/9880566

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1999-2-11
pubmed:databankReference
pubmed:abstractText
Phosphatidylglycerophosphate (PGP) synthase catalyzes the first step in the cardiolipin (CL) branch of phospholipid biosynthesis in mammalian cells. In this study, we isolated a Chinese hamster ovary (CHO) cDNA encoding a putative protein similar in sequence to the yeast PGS1 gene product, PGP synthase. The gene for the isolated CHO cDNA was named PGS1. Expression of the CHO PGS1 cDNA in CHO-K1 cells and production of a recombinant CHO PGS1 protein with a N-terminal extension in Escherichia coli resulted in 15-fold and 90-fold increases of PGP synthase specific activity, respectively, establishing that CHO PGS1 encodes PGP synthase. A PGP synthase-defective CHO mutant, PGS-S, isolated previously (Ohtsuka, T., Nishijima, M., and Akamatsu, Y. (1993) J. Biol. Chem. 268, 22908-22913) exhibits striking reductions in biosynthetic rate and cellular content of phosphatidylglycerol (PG) and CL and shows mitochondrial morphological and functional abnormalities. The CHO PGS-S mutant transfected with the CHO PGS1 cDNA exhibited 620-fold and 7-fold higher PGP synthase activity than mutant PGS-S and wild type CHO-K1 cells, respectively, and had a normal cellular content and rate of biosynthesis of PG and CL. In contrast to mutant PGS-S, the transfectant had morphologically normal mitochondria. When the transfectant and mutant PGS-S cells were cultivated in a glucose-depleted medium, in which cellular energy production mainly depends on mitochondrial function, the transformant but not mutant PGS-S was capable of growth. These results demonstrated that the morphological and functional defects displayed by the PGS-S mutant are due directly to the reduced ability to make normal levels of PG and/or CL.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
274
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1828-34
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9880566-Amino Acid Sequence, pubmed-meshheading:9880566-Animals, pubmed-meshheading:9880566-Base Sequence, pubmed-meshheading:9880566-CHO Cells, pubmed-meshheading:9880566-Cardiolipins, pubmed-meshheading:9880566-Cricetinae, pubmed-meshheading:9880566-DNA, Complementary, pubmed-meshheading:9880566-Humans, pubmed-meshheading:9880566-Microscopy, Electron, pubmed-meshheading:9880566-Mitochondria, pubmed-meshheading:9880566-Molecular Sequence Data, pubmed-meshheading:9880566-Mutation, pubmed-meshheading:9880566-Oxidative Phosphorylation, pubmed-meshheading:9880566-Phosphatidylglycerols, pubmed-meshheading:9880566-RNA, Messenger, pubmed-meshheading:9880566-Saccharomyces cerevisiae, pubmed-meshheading:9880566-Sequence Alignment, pubmed-meshheading:9880566-Transferases (Other Substituted Phosphate Groups)
pubmed:year
1999
pubmed:articleTitle
Isolation of a chinese hamster ovary (CHO) cDNA encoding phosphatidylglycerophosphate (PGP) synthase, expression of which corrects the mitochondrial abnormalities of a PGP synthase-defective mutant of CHO-K1 cells.
pubmed:affiliation
Department of Biochemistry and Cell Biology, National Institute of Infectious Diseases, Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't