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Allele-specific suppression of a Saccharomyces cerevisiae prp20 mutation by overexpression of a nuclear serine/threonine protein kinase.
Journal article

Allele-specific suppression of a Saccharomyces cerevisiae prp20 mutation by overexpression of a nuclear serine/threonine protein kinase.

  • 1996-03-20
Published in:
  • Molecular & general genetics : MGG. - 1996
Alleles
Amino Acid Sequence
Base Sequence
Cell Nucleus
DNA-Binding Proteins
Fungal Proteins
Gene Expression
Guanine Nucleotide Exchange Factors
Molecular Sequence Data
Mutagenesis
Nuclear Proteins
Plasmids
Protein-Serine-Threonine Kinases
Restriction Mapping
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Schizosaccharomyces
Sequence Deletion
Sequence Homology, Amino Acid
Suppression, Genetic
English 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.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/66846
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