Source:http://linkedlifedata.com/resource/pubmed/id/11746600
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15
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pubmed:dateCreated |
2001-12-17
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pubmed:abstractText |
Glycosylphosphatidylinositols (GPIs) are found in all eukaryotes and are synthesized in a pathway that starts with the transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to phosphatidylinositol (PI). This reaction is carried out by a protein complex, three of whose subunits in humans, hGpi1p, Pig-Cp and Pig-Ap, have sequence and functional homologues in the Saccharomyces cerevisiae Gpi1, Gpi2 and Gpi3 proteins, respectively. Human GlcNAc-PI synthase contains two further subunits, Pig-Hp and PigPp. We report that the essential YNL038w gene encodes the S. cerevisiae homologue of Pig-Hp. Haploid YNL038w-deletion strains were created, in which Ynl038wp could be depleted by repressing YNL038w expression using the GAL10 promoter. Depletion of Ynl038wp from membranes virtually abolished in vitro GlcNAc-PI synthetic activity, indicating that Ynl038wp is necessary for GlcNAc-PI synthesis in vitro. Further, depletion of Ynl038wp in an smp3 mutant background prevented the formation of the trimannosylated GPI intermediates that normally accumulate in this late-stage GPI assembly mutant. Ynl038wp is therefore required for GPI synthesis in vivo. Because YNL038w encodes a protein involved in GPI biosynthesis, we designate the gene GPI15. Potential Pig-Hp/Gpi15p counterparts are also encoded in the genomes of Schizosacchomyces pombe and Candida albicans.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylglucosamine,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylphosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/N-acetylglucosaminylphosphatidylinos...,
http://linkedlifedata.com/resource/pubmed/chemical/PIGH protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0749-503X
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2001 John Wiley & Sons, Ltd.
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pubmed:issnType |
Print
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1383-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11746600-Acetylglucosamine,
pubmed-meshheading:11746600-Amino Acid Sequence,
pubmed-meshheading:11746600-Chromatography, Thin Layer,
pubmed-meshheading:11746600-Glycosylphosphatidylinositols,
pubmed-meshheading:11746600-Membrane Proteins,
pubmed-meshheading:11746600-Molecular Sequence Data,
pubmed-meshheading:11746600-Mutagenesis,
pubmed-meshheading:11746600-Phosphatidylinositols,
pubmed-meshheading:11746600-Saccharomyces cerevisiae,
pubmed-meshheading:11746600-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11746600-Sequence Alignment,
pubmed-meshheading:11746600-Sequence Homology, Amino Acid
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pubmed:year |
2001
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pubmed:articleTitle |
Ynl038wp (Gpi15p) is the Saccharomyces cerevisiae homologue of human Pig-Hp and participates in the first step in glycosylphosphatidylinositol assembly.
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pubmed:affiliation |
Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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