Abstract
Glycosylphosphatidylinositol (GPI) anchoring is the main mechanism allowing proper localization of secretory proteins in cell membranes. We have isolated an Aspergillus nidulans homolog of the human PIG-P gene, which encodes a subunit of acetylglucosaminyltransferase (GPI-GnT)-an enzyme involved in the synthesis of GPI anchors. A. nidulans pigP mutants have significantly decreased GPI synthesis. On solid media they show strong growth retardation (the "button" phenotype) while in liquid minimal media they show overall good growth but with hyperbranched and bulbous hyphae with impaired septation. Furthermore, the pigP strains, in contrast to the wild-type, abundantly secrete a 33-kDa alkaline serine protease (ALP) into the liquid medium.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Aspergillus nidulans / enzymology*
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Aspergillus nidulans / genetics
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Aspergillus nidulans / growth & development
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Cloning, Molecular
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DNA, Fungal / chemistry
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DNA, Fungal / genetics
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DNA, Fungal / isolation & purification
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Fungal Proteins / genetics
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Fungal Proteins / metabolism*
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Glycosylphosphatidylinositols / biosynthesis
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Microscopy, Confocal
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Molecular Sequence Data
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Mutation
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Mycelium / enzymology*
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Mycelium / genetics
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Mycelium / growth & development
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N-Acetylglucosaminyltransferases / genetics
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N-Acetylglucosaminyltransferases / isolation & purification
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N-Acetylglucosaminyltransferases / metabolism*
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Sequence Analysis, DNA
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Sequence Homology, Amino Acid
Substances
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DNA, Fungal
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Fungal Proteins
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Glycosylphosphatidylinositols
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N-Acetylglucosaminyltransferases
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N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase