Abstract
Three type II membrane proteins Anp1, Van1 and Mnn9 of Saccharomyces cerevisiae share significant sequence homology. Their precise biochemical activity has long been unknown though the mutant phenotype indicates their participation in protein glycosylation in the Golgi apparatus. To shed light on their molecular characteristics, interactions of these proteins were studied by immunoprecipitation after solubilizing the membrane by nonionic detergent. Our results indicated that there are at least two submembrane complexes containing these proteins: one contains Van1 and Mnn9 proteins and the other contains Anp1 and Mnn9 proteins. In addition, Hoc1 protein which has significant homology to Och1 protein colocalized with Anp1 and Mnn9 proteins. These complexes with similar but partially different constituents may represent essential parts of glycosylation machinery in the yeast Golgi compartments.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Alleles
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Fungal Proteins / analysis
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Fungal Proteins / genetics
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Fungal Proteins / metabolism*
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Genes, Fungal
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Glycosylation
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Golgi Apparatus / genetics
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Golgi Apparatus / metabolism*
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Macromolecular Substances
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Membrane Glycoproteins / analysis
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Membrane Glycoproteins / genetics
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Membrane Glycoproteins / metabolism
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Membrane Proteins / analysis
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Multigene Family
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Mutagenesis
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Precipitin Tests
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Proto-Oncogene Proteins c-myc / genetics
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Recombinant Fusion Proteins / metabolism
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / isolation & purification
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins*
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Vanadates / pharmacology
Substances
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Fungal Proteins
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MNN9 protein, S cerevisiae
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Macromolecular Substances
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Membrane Glycoproteins
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Membrane Proteins
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Proto-Oncogene Proteins c-myc
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Recombinant Fusion Proteins
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Saccharomyces cerevisiae Proteins
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Vanadates