title: Synthetic model peptides phosphorylated in vitro by NII kinase and cation-mediated interactions with DNA.
abstract: Minimum substrate requirements for nuclear NII kinase (casein II kinase) were analyzed with synthetic peptides modeled according to amino acid composition of phosphopeptides isolated from chromatin. Uncharged blocked peptide termini decreased the requirement for acidic clusters neighboring the phosphate acceptor amino acid (serine) such that only one group immediately N-terminal to serine was sufficient for kinase activity. Studies on peptide interaction with DNA showed that the model phosphopeptides bound to DNA only in the phosphorylated form suggesting involvement of phosphorylation in protein-DNA interactions yet to be identified.
authors.affiliation: Institute of Cell Biology, University of Perugìa, Italy.
authors.forename: G L
authors.initials: GL
authors.lastname: Gianfranceschi
authors.forename: E
authors.initials: E
authors.lastname: Cardellini
authors.forename: G
authors.initials: G
authors.lastname: Piccinini
authors.forename: M
authors.initials: M
authors.lastname: Bramucci
authors.forename: A
authors.initials: A
authors.lastname: Miano
authors.forename: E
authors.initials: E
authors.lastname: Maccari
authors.forename: D
authors.initials: D
authors.lastname: Amici
authors.forename: E
authors.initials: E
authors.lastname: Durban
mesh_terms: D000595:Amino Acid Sequence; D010582:Bacteriophage lambda / Q000378:metabolism; D002412:Cations; D004247:DNA / Q000737:chemistry*; D004279:DNA, Viral / Q000378:metabolism; D008956:Models, Chemical; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D010766:Phosphorylation; D010768:Phosphoserine / Q000737:chemistry; D011494:Protein Kinases / Q000378:metabolism*; D014158:Transcription, Genetic
chemical_list: D002412:Cations; D004279:DNA, Viral; D010455:Peptides; D010768:Phosphoserine; D004247:DNA; D011494:Protein Kinases; C026813:protein kinase NII