Ref ID : 4883
Phillip E. Ryals; Protein Prenylation in Tetrahymena. Arch.Protistenk 147:199-204, 1996
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Tetrahymena vorax V2S and Tetrahymena pyriformis GL were examined for the presence of proteins covalently modified with mevalonate-derived lipids. Radiolabeling of cells using [3H]mevalonolactone, [3H]mevalonate, [3H]farnesyl pyrophosphate or [3H]geranylgeranyl pyrophosphate resulted in the appearance protein-associated radioactivity following protein delipidation in acetone. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of labeled protein revealed radioactive polypeptides ranging in molecular mass from 123 to 14 kDa following scintillation counting of gel slices or fluorography. Methyl iodide cleavage of total labeled protein followed by HPLC analysis and scintillation counting of the released prenyl alcohols showed radioactive peaks that co-chromatographed with commercially obtained farnesol (C15) and geranylgeraniol (C20).