Nakajo S, Masuda Y, Nakaya K, Nakamura Y
Laboratory of Biological Chemistry, School of Pharmaceutical Sciences, Showa University, Tokyo.
J Biochem. 1988 Dec;104(6):946-51. doi: 10.1093/oxfordjournals.jbchem.a122588.
Calmodulin is specifically phosphorylated by casein kinase 2 (CK 2), but not by casein kinase 1, A kinase, or C kinase. In the present report, the stoichiometry of the phosphorylation of calmodulin by CK 2 in the presence and absence of polylysine and its phosphorylation sites were examined. In the absence of polylysine, the radioactive phosphate incorporated into calmodulin by CK 2 was only 0.01 mol/mol and the phosphorylation occurred at Ser-101. In the presence of polylysine, 1.2 mol of radioactive phosphate was incorporated into 1 mol of calmodulin. In this case, Thr-79 in addition to Ser-101 was phosphorylated, but Ser-81 was not. The sequence around the phosphorylated Thr is Asp-Thr(P)-Asp-Ser-Glu-Glu-Glu-.
钙调蛋白可被酪蛋白激酶2(CK 2)特异性磷酸化,但不能被酪蛋白激酶1、A激酶或C激酶磷酸化。在本报告中,研究了在有和没有多聚赖氨酸存在的情况下CK 2对钙调蛋白磷酸化的化学计量关系及其磷酸化位点。在没有多聚赖氨酸的情况下,CK 2掺入钙调蛋白的放射性磷酸盐仅为0.01摩尔/摩尔,磷酸化发生在丝氨酸101位点。在有多聚赖氨酸存在的情况下,1摩尔钙调蛋白掺入了1.2摩尔放射性磷酸盐。在这种情况下,除了丝氨酸101外,苏氨酸79也发生了磷酸化,但丝氨酸81未被磷酸化。磷酸化苏氨酸周围的序列为天冬氨酸-苏氨酸(P)-天冬氨酸-丝氨酸-谷氨酸-谷氨酸-谷氨酸-。