Abstract
Saccharomyces cerevisiae uso1-1 mutant stops the transport of secretory proteins from the endoplasmic reticulum to the Golgi apparatus at 37 degrees C. We found that this temperature-sensitive defect was suppressed either by increasing the concentration of calcium ion in the medium or by introducing in the cell the SLY genes which suppress the defect of Ypt1 protein, a small GTP-binding protein. The common phenotype and suppression of the mutants suggest that Uso1 and Ypt1 proteins function in the same process of protein transport, i.e., targeting or fusion of the transport vesicles to the Golgi membrane.
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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Amino Acid Sequence
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Calcium / pharmacology*
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Calcium Chloride / pharmacology
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Carrier Proteins*
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Consensus Sequence
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Egtazic Acid / pharmacology
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Fungal Proteins / biosynthesis
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Fungal Proteins / genetics*
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GTP Phosphohydrolases / biosynthesis*
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GTP-Binding Proteins / biosynthesis*
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Genes, Fungal*
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Magnesium Chloride / pharmacology
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Molecular Sequence Data
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Phenotype
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Saccharomyces cerevisiae / drug effects
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / growth & development*
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Saccharomyces cerevisiae Proteins*
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Sequence Homology, Amino Acid
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Suppression, Genetic
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Temperature
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Vesicular Transport Proteins*
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rab GTP-Binding Proteins*
Substances
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Carrier Proteins
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Fungal Proteins
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Saccharomyces cerevisiae Proteins
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USO1 protein, S cerevisiae
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Vesicular Transport Proteins
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Magnesium Chloride
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Egtazic Acid
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GTP Phosphohydrolases
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GTP-Binding Proteins
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YPT1 protein, S cerevisiae
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rab GTP-Binding Proteins
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Calcium Chloride
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Calcium