title: Synthesis and screening of a CaaL peptide library versus FTase reveals a surprising number of substrates.
abstract: Proteins bearing a CaaL sequence are typically geranylgeranylated to enable their proper localization and function. We found that many of the dansyl-GCaaL peptides representing mammalian CaaL proteins can be farnesylated by FTase. This result may have important implications for prenylated protein biology.
authors.affiliation: Department of Medicinal Chemistry and Molecular Pharmacology and Center for Cancer Research, Purdue University, West Lafayette, IN 47907, United States.
authors.forename: Amanda J
authors.initials: AJ
authors.lastname: Krzysiak
authors.forename: Animesh V
authors.initials: AV
authors.lastname: Aditya
authors.forename: James L
authors.initials: JL
authors.lastname: Hougland
authors.forename: Carol A
authors.initials: CA
authors.lastname: Fierke
authors.forename: Richard A
authors.initials: RA
authors.lastname: Gibbs
mesh_terms: D019883:Alkyl and Aryl Transferases / Q000378:metabolism; D000595:Amino Acid Sequence; D051231:Farnesyltranstransferase / Q000378:metabolism*; D019151:Peptide Library; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D054876:Prenylation; D013379:Substrate Specificity; D018631:ras Proteins / Q000378:metabolism
chemical_list: D019151:Peptide Library; D010455:Peptides; D019883:Alkyl and Aryl Transferases; C083291:geranylgeranyltransferase type-I; D051231:Farnesyltranstransferase; D018631:ras Proteins