title: Protein prenylation in Schizosaccharomyces pombe.
abstract: S. pombe is shown to be a powerful system for studies concerning attachment of polyisoprenoid moieties to proteins, due to its ability to take up exogenous mevalonic acid efficiently. The fission yeast can take up about 5% of the exogenously added mevalonic acid and incorporate approximately 10% of this into protein. By contrast, the uptake obtained with the budding yeast S. cerevisiae is less than 0.5%. HPLC analysis of total S. pombe protein-bound isoprenoids revealed that approximately 55% of the counts co-migrated with the geranylgeraniol standard, while approximately 45% of the counts co-migrated with farnesol. We could not detect any effects of mevinolin or other HMG-CoA reductase inhibitors in S. pombe.
authors.affiliation: Laboratory of Eukaryotic Molecular Genetics, National Institute for Medical Research, The Ridgeway, Mill Hill, London, UK.
authors.forename: T
authors.initials: T
authors.lastname: Giannakouros
authors.forename: J
authors.initials: J
authors.lastname: Armstrong
authors.forename: A I
authors.initials: AI
authors.lastname: Magee
mesh_terms: D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000378:metabolism*; D008798:Mevalonic Acid / Q000378:metabolism; D012568:Schizosaccharomyces / Q000378:metabolism*
chemical_list: D005656:Fungal Proteins; D008798:Mevalonic Acid