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PMID:8676864

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Citation

Fleischmann, M, Stagljar, I and Aebi, M (1996) Allele-specific suppression of a Saccharomyces cerevisiae prp20 mutation by overexpression of a nuclear serine/threonine protein kinase. Mol. Gen. Genet. 250:614-25

Abstract

The yeast PRP20 protein is homologous to the RCC1 protein of higher eukaryotes and is required for mRNA export and maintenance of nuclear structure. RCC1/PRP20 act as guanine nucleotide exchange factors for the nuclear Ras-like Ran/GSP1 proteins. In a search for prp20-10 allele-specific high-copy-number suppressors, the KSP1 locus, encoding a serine/threonine protein kinase was isolated. Ksp1p is a nuclear protein that is not essential for vegetative growth of yeast. Inactivation of the kinase activity by a mutation affecting the catalytic center of the Ksp1p eliminated the suppressing activity. Based on the isolation of a protein kinase as a high-copy-number suppressor, the phosphorylation of Prp20p was examined. In vivo labeling experiments showed that Prp20p is a phosphoprotein; however, deletion of the KSP1 kinase did not affect Prp20p phosphorylation.

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Keywords

Alleles; Amino Acid Sequence; Base Sequence; Cell Nucleus/enzymology; DNA-Binding Proteins/genetics; Fungal Proteins/genetics; Gene Expression; Guanine Nucleotide Exchange Factors; Molecular Sequence Data; Mutagenesis; Nuclear Proteins/genetics; Plasmids; Protein-Serine-Threonine Kinases/biosynthesis; Protein-Serine-Threonine Kinases/genetics; Restriction Mapping; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae Proteins; Schizosaccharomyces/enzymology; Schizosaccharomyces/genetics; Sequence Deletion; Sequence Homology, Amino Acid; Suppression, Genetic

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