Phosphoserine in peptide substrates can specify casein kinase II action.
Casein kinase II is a ubiquitous serine/threonine protein kinase which utilizes acidic amino acid residues as recognition determinants in its substrates, the motif -S/T-X-X-D/E- being particularly important. To test whether a phosphoserine residue can act as a substrate determinant, a peptide was synthesized, containing the sequence -S-X-X-S, which was not phosphorylated by casein kinase II. However, upon phosphorylation at the +3 position, the peptide became a substrate for casein kinase II. With another peptide, a positive influence of more distal phosphorylations was found. The results indicate the potential for casein kinase II to participate in hierarchal phosphorylation schemes.
Hrubey
T W
TW
Department of Biochemistry and Molecular Biology Indiana University School of Medicine, Indianapolis 46223.
Roach
P J
PJ
D000595:Amino Acid Sequence; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D047388:Casein Kinases; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis; D010748:Phosphopeptides / Q000138:chemical synthesis / Q000302:isolation & purification; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D012694:Serine; D013379:Substrate Specificity
D009842:Oligopeptides; D010748:Phosphopeptides; D012694:Serine; D011494:Protein Kinases; D047388:Casein Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases