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Protein prenylation in Schizosaccharomyces pombe
Author(s) -
Giannakouros Thomas,
Armstrong John,
Magee Anthony I.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80337-g
Subject(s) - schizosaccharomyces pombe , geranylgeraniol , mevalonic acid , farnesol , yeast , prenylation , biochemistry , reductase , saccharomyces cerevisiae , budding yeast , chemistry , schizosaccharomyces , biology , enzyme
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 .

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