title: Ras protein of the slime mold Physarum polycephalum is farnesylated in vitro.
abstract: 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.
authors.affiliation: Institut of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa.
authors.forename: E
authors.initials: E
authors.lastname: Talarczyk
authors.forename: V S
authors.initials: VS
authors.lastname: Hung
authors.forename: P
authors.initials: P
authors.lastname: Kozlowski
authors.forename: J
authors.initials: J
authors.lastname: Trzcinska-Danielewicz
authors.forename: E
authors.initials: E
authors.lastname: Swiezewska
mesh_terms: 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*
chemical_list: D005656:Fungal Proteins; D004122:Dimethylallyltranstransferase; D018631:ras Proteins