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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
44
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pubmed:dateCreated |
1996-12-26
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pubmed:databankReference | |
pubmed:abstractText |
The temperature-sensitive Saccharomyces cerevisiae gpi1 mutant is blocked in [3H]inositol incorporation into protein and defective in the synthesis of N-acetylglucosaminylphosphatidylinositol, the first step in glycosylphosphatidylinositol (GPI) anchor assembly (Leidich, S. D., Drapp, D. A., and Orlean, P. (1994) J. Biol. Chem. 269, 10193-10196). The GPI1 gene, which encodes a 609-amino acid membrane protein, was cloned by complementation of the temperature sensitivity of gpi1 and corrects the mutant's [3H]inositol labeling and enzymatic defects. Disruption of GPI1 yields viable haploid cells that are temperature-sensitive for growth, for [3H]inositol incorporation into protein, and for GPI anchor-dependent processing of the Gas1/Ggp1 protein and that lack in vitro N-acetylglucosaminylphosphatidylinositol synthetic activity. The Gpi1 protein thus participates in GPI synthesis and is required for growth at 37 degrees C. When grown at a semipermissive temperature of 30 degrees C, gpi1 cells and gpi1::URA3 disruptants form large, round, multiply budded cells with a separation defect. Homozygous gpi1/gpi1, gpi1::URA3/gpi1::URA3, gpi2/gpi2, and gpi3/gpi3 diploids undergo meiosis, but are defective in ascospore wall maturation for they fail to give the fluorescence due to the dityrosine-containing layer in the ascospore wall. These findings indicate that GPIs have key roles in the morphogenesis and development of S. cerevisiae.
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pubmed:grant | |
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 |
Nov
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
27829-37
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8910381-Amino Acid Sequence,
pubmed-meshheading:8910381-Base Sequence,
pubmed-meshheading:8910381-Carbohydrate Sequence,
pubmed-meshheading:8910381-Cloning, Molecular,
pubmed-meshheading:8910381-Genes, Fungal,
pubmed-meshheading:8910381-Glycosylphosphatidylinositols,
pubmed-meshheading:8910381-Homozygote,
pubmed-meshheading:8910381-Inositol,
pubmed-meshheading:8910381-Kinetics,
pubmed-meshheading:8910381-Membrane Proteins,
pubmed-meshheading:8910381-Molecular Sequence Data,
pubmed-meshheading:8910381-Mutation,
pubmed-meshheading:8910381-Restriction Mapping,
pubmed-meshheading:8910381-Saccharomyces cerevisiae,
pubmed-meshheading:8910381-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8910381-Spores, Fungal,
pubmed-meshheading:8910381-Temperature
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pubmed:year |
1996
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pubmed:articleTitle |
Gpi1, a Saccharomyces cerevisiae protein that participates in the first step in glycosylphosphatidylinositol anchor synthesis.
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pubmed:affiliation |
Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA. p-orlean@uiuc.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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