| In vitro biosynthesis of glycosylphosphatidylinositol in Aspergillus fumigatus. | |
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MedLine Citation:
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PMID: 15568819 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Glycosylphosphatidylinositol (GPI) represents a mechanism for the attachment of proteins to the plasma membrane found in all eukaryotic cells. GPI biosynthesis has been mainly studied in parasites, yeast, and mammalian cells. Aspergillus fumigatus, a filamentous fungus, produces GPI-anchored molecules, some of them being essential in the construction of the cell wall. An in vitro assay was used to study the GPI biosynthesis in the mycelium form of this organism. In the presence of UDP-GlcNAc and coenzyme A, the cell-free system produces the initial intermediates of the GPI biosynthesis: GlcNAc-PI, GlcN-PI, and GlcN-(acyl)PI. Using GDP-Man, two types of mannosylation are observed. First, one or two mannose residues are added to GlcN-PI. This mannosylation, never described in fungi, does not require dolichol phosphomannoside (Dol-P-Man) as the monosaccharide donor. Second, one to five mannose residues are added to GlcN-(acyl)PI using Dol-P-Man as the mannose donor. The addition of ethanolamine phosphate groups to the first, second, and third mannose residue is also observed. This latter series of GPI intermediates identified in the A. fumigatus cell-free system indicates that GPI biosynthesis in this filamentous fungus is similar to the mammalian or yeast systems. Thus, these biochemical data are in agreement with a comparative genome analysis that shows that all but 3 of the 21 genes described in the Saccharomyces cerevisiae GPI pathways are found in A. fumigatus. |
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Authors:
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Thierry Fontaine; Terry K Smith; Arthur Crossman; John S Brimacombe; Jean-Paul Latgé; Michael A J Ferguson |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biochemistry Volume: 43 ISSN: 0006-2960 ISO Abbreviation: Biochemistry Publication Date: 2004 Dec |
Date Detail:
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Created Date: 2004-11-30 Completed Date: 2005-01-21 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: United States |
Other Details:
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Languages: eng Pagination: 15267-75 Citation Subset: IM |
Affiliation:
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Unité des Aspergillus, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France. tfontain@pasteur.fr |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Acetylglucosamine
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analogs & derivatives*,
biosynthesis,
chemistry Acylation Adenosine Triphosphate / chemistry Aspergillus fumigatus / chemistry, metabolism* Carbohydrate Sequence Coenzyme A / metabolism Ethanolamines / metabolism Ethylmaleimide / chemistry Glycolipids / biosynthesis Glycosylphosphatidylinositols / biosynthesis* Guanosine Diphosphate Mannose / metabolism Inositol / analogs & derivatives*, biosynthesis, metabolism Lipopeptides Molecular Sequence Data Oligopeptides / chemistry Phosphatidylinositols / biosynthesis, chemistry Uridine Diphosphate N-Acetylglucosamine / biosynthesis |
| Chemical | |
Reg. No./Substance:
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0/Ethanolamines; 0/GlcNalpha1-6-myo-inositol-1-HPO4-sn-1, 2-dipalmitoylglycerol; 0/Glycolipids; 0/Glycosylphosphatidylinositols; 0/Lipopeptides; 0/N-acetylglucosaminylphosphatidylinositol; 0/Oligopeptides; 0/Phosphatidylinositols; 1071-23-4/phosphorylethanolamine; 128-53-0/Ethylmaleimide; 1402-82-0/amphomycin; 3123-67-9/Guanosine Diphosphate Mannose; 528-04-1/Uridine Diphosphate N-Acetylglucosamine; 56-65-5/Adenosine Triphosphate; 6917-35-7/Inositol; 7512-17-6/Acetylglucosamine; 85-61-0/Coenzyme A |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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