Document Detail


In vitro biosynthesis of glycosylphosphatidylinositol in Aspergillus fumigatus.
MedLine Citation:
PMID:  15568819     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Thierry Fontaine; Terry K Smith; Arthur Crossman; John S Brimacombe; Jean-Paul Latgé; Michael A J Ferguson
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemistry     Volume:  43     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  2004 Dec 
Date Detail:
Created Date:  2004-11-30     Completed Date:  2005-01-21     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  15267-75     Citation Subset:  IM    
Affiliation:
Unité des Aspergillus, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France. tfontain@pasteur.fr
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MeSH Terms
Descriptor/Qualifier:
Acetylglucosamine / 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:
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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