Protein prenylation in Schizosaccharomyces pombe

FEBS Letters

Magee, Anthony I.¹  Armstrong, John²  Giannakouros, Thomas¹ 

[1] Laboratory of Eukaryotic Molecular Genetics, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK;Membrane Molecular Biology Laboratory, Imperial Cancer Research Fund, P.O. Box 123, Lincoln's Inn Fields, London WC2A 3PX, UK

关键词: S. pombe;    S. cerevisiae;    Mevalonic acid;    Prenylated protein;    HMG-CoA;    hydroxymethylglutaryl coenzyme A;    MVA;    mevalonic acid;    SDS;    sodium dodecyl sulphate;    TCA;    trichloroacetic acid;   

DOI  :  10.1016/0014-5793(92)80337-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

S. pombe is shown to be a powerful system for studies concerning attachment or 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 ∼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 ∼55% of the counts co-migrated with the geranylgeraniol standard, while ∼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.

【 授权许可】

Unknown