Ras protein of the slime mold Physarum polycephalum is farnesylated in vitro.
Physarum Ppras1 protein was efficiently prenylated by prenyltransferases of spinach. Surprisingly in spite of the C-terminal sequence (CLLL) specific for geranylgeranylation the protein was preferentially farnesylated. Consequences of this observation are discussed.
Talarczyk
E
E
Institut of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa.
Hung
V S
VS
Kozlowski
P
P
Trzcinska-Danielewicz
J
J
Swiezewska
E
E
D000595:Amino Acid Sequence; D000818:Animals; D004122:Dimethylallyltranstransferase / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism*; D016839:Physarum polycephalum / Q000378:metabolism*; D017368:Protein Prenylation; D018724:Spinacia oleracea / Q000201:enzymology; D013379:Substrate Specificity; D018631:ras Proteins / Q000737:chemistry / Q000378:metabolism*
D005656:Fungal Proteins; D004122:Dimethylallyltranstransferase; D018631:ras Proteins