Lück-Vielmetter D, Schleicher M, Grabatin B, Wippler J, Gerisch G
Max-Planck-Institut für Biochemie, Martinsried, FRG.
FEBS Lett. 1990 Aug 20;269(1):239-43. doi: 10.1016/0014-5793(90)81163-i.
The target sites of soluble myosin heavy chain kinases partially purified from growth phase or aggregation competent cells of Dictyostelium discoideum were identified by the use of normal and mutated fragments of the myosin heavy chain. The kinases from both developmental stages phosphorylated two previously established threonine residues, as well as an additional one. The newly identified site is located within the putative core region of the coiled-coil formed by the myosin tail. A lysine following the phosphorylated threonine residue is the only common feature of the sequences around these sites. The kinases, which specifically phosphorylate threonine residues in wild-type myosin, did accept serine if it was in the right structural context.
通过使用肌球蛋白重链的正常片段和突变片段，确定了从盘基网柄菌生长阶段或聚集感受态细胞中部分纯化的可溶性肌球蛋白重链激酶的靶位点。来自这两个发育阶段的激酶使两个先前确定的苏氨酸残基以及另一个残基发生磷酸化。新确定的位点位于由肌球蛋白尾部形成的卷曲螺旋的假定核心区域内。磷酸化苏氨酸残基后的赖氨酸是这些位点周围序列的唯一共同特征。那些特异性磷酸化野生型肌球蛋白中苏氨酸残基的激酶，如果丝氨酸处于正确的结构环境中，也会接受它。
