title: Farnesylation of Batten disease CLN3 protein.
abstract: The carboxyl terminal of the predicted amino acid sequence of the Batten disease CLN3 gene protein is CQLS. This motif is expected to be a site for farnesylation at the cysteine residue. In order to determine whether this is indeed farnesylated we have carried out the in-vitro prenylation of tetrapeptides CVLS, CAIL and CQLS using a farnesyl transferase preparation from bovine brain. The data shows that the CQLS is a good acceptor of a farnesyl group similar to CVLS while it is a poor acceptor of a geranylgeranyl group unlike CAIL, which is a good acceptor of a geranylgeranyl group. This suggests that the CLN3 gene product may be a farnesylated protein.
authors.affiliation: New York State Office of Mental Retardation and Development Disabilities, Institute for Basic Research in Developmental Disabilities, Staten Island 10314-6399, USA.
authors.forename: R K
authors.initials: RK
authors.lastname: Pullarkat
authors.forename: G N
authors.initials: GN
authors.lastname: Morris
mesh_terms: D000293:Adolescent; D019883:Alkyl and Aryl Transferases; D000818:Animals; D001921:Brain / Q000201:enzymology; D002417:Cattle; D002648:Child; D002675:Child, Preschool; D016213:Cyclins; D051231:Farnesyltranstransferase; D015971:Gene Expression Regulation, Enzymologic / Q000502:physiology; D006801:Humans; D007223:Infant; D008562:Membrane Glycoproteins / Q000235:genetics*; D018895:Microsatellite Repeats / Q000235:genetics; D018832:Molecular Chaperones / Q000235:genetics*; D009472:Neuronal Ceroid-Lipofuscinoses / Q000201:enzymology / Q000235:genetics*; D017368:Protein Prenylation / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins; D014166:Transferases / Q000235:genetics
chemical_list: C079895:CLN3 protein, S cerevisiae; C105199:CLN3 protein, human; D016213:Cyclins; D008562:Membrane Glycoproteins; D018832:Molecular Chaperones; D029701:Saccharomyces cerevisiae Proteins; D014166:Transferases; D019883:Alkyl and Aryl Transferases; D051231:Farnesyltranstransferase