Hotta Y, Stern H
Eur J Biochem. 1979 Mar 15;95(1):31-8. doi: 10.1111/j.1432-1033.1979.tb12936.x.
Properties of the helix-destabilizing protein from Lilium meiotic cells, 'R-protein', have been examined after treating it either with alkaline phosphatase or with two types of protein kinase. Dephosphorylation with the phosphatase increases binding capacity for single-strand DNA, but abolishes specificity of binding. Dephosphorylated R-protein binds equally to single and double-strand DNA. The capacity to facilitate denaturation or renaturation of DNA is also abolished by the treatment, but cooperativity characteristics are unaffected. The consequences of protein kinase treatment of native or dephosphorylated R-protein depend upon the origin of the kinase. Heterologous cyclic-AMP-dependent protein kinase cannot reverse the effects of dephosphorylation. However, it abolishes the binding affinity of either native or dephosphorylated R-protein for DNA. A protein kinase isolated from meiotic cells has no effect on the native protein, but it does restore all native properties tested to the dephosphorylated form after phosphorylating approximately two residues/molecule of protein.
对来自百合减数分裂细胞的解旋稳定蛋白“R蛋白”分别用碱性磷酸酶或两种蛋白激酶处理后，对其特性进行了检测。用磷酸酶去磷酸化可增加其与单链DNA的结合能力，但会消除结合的特异性。去磷酸化的R蛋白与单链和双链DNA的结合能力相同。该处理还会消除其促进DNA变性或复性的能力，但协同特性不受影响。对天然或去磷酸化的R蛋白进行蛋白激酶处理的结果取决于激酶的来源。异源环磷酸腺苷依赖性蛋白激酶不能逆转去磷酸化的作用。然而，它会消除天然或去磷酸化的R蛋白对DNA的结合亲和力。从减数分裂细胞中分离出的一种蛋白激酶对天然蛋白没有影响，但在每分子蛋白磷酸化大约两个残基后，它确实能使去磷酸化形式的所有测试天然特性得以恢复。
