Identification of peptides mimicking the ligands of proteins phosphorylated by protein kinase CK2

• Published in: Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2004-02, Vol.25 (2), p.191-197
• Main Authors: Cardellini, Elena, Felici, Franco, Gianfranceschi, Gian Luigi
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Binding Sites; Biological and medical sciences; Casein Kinase II; DNA Topoisomerases, Type I - metabolism; Fundamental and applied biological sciences. Psychology; Humans; Molecular Sequence Data; Peptide Library; Peptides - metabolism; Phage libraries; Phosphorylation; Protein Binding; Protein kinase CK2; Protein-Serine-Threonine Kinases - metabolism; RNA Polymerase II - metabolism; Synthetic peptides; Vertebrates: endocrinology
• ISSN: 0196-9781; 1873-5169
• DOI: 10.1016/j.peptides.2003.12.017

Synthetic peptides containing a phosphorylation site for protein kinase CK2 were used to investigate their binding properties to other peptides/proteins. The aim of this work was to find an efficient procedure to search for these peptide/protein ligands. The goal was successfully achieved through screening of random peptide libraries displayed on phage. Peptides corresponding to the amino terminal region of topoisomerase I were synthesized in both phosphorylated and unphosphorylated form and used to screen the libraries. Four of the selected sequences were also tested for their reactivity with synthetic peptides corresponding to the carboxy terminal region of the largest subunit of RNA polymerase II. The positive reaction detected supports the hypothesis that the isolated sequences may represent mimics of ligands of proteins phosphorylated by protein kinase CK2.