Palvimo J, Linnala-Kankkunen A, Mäenpää P H
Biochem Biophys Res Commun. 1985 Nov 27;133(1):343-6. doi: 10.1016/0006-291x(85)91881-9.
The effect of phosphorylation on the affinity of HMG 14 from calf thymus for single-stranded DNA (ssDNA) was studied, using a cyclic GMP-dependent protein kinase from bovine lung and a nuclear protein kinase II from rat liver. When phosphorylated by G-kinase, HMG 14 eluted at 0.27 M NaCl from the ssDNA-column, whereas the native protein eluted at 0.30 M salt concentration. In contrast, phosphorylation by nuclear protein kinase II did not alter dissociation of HMG 14 from ssDNA and the phosphoprotein consequently coeluted with the native HMG 14. Thus, addition of a negative charge by phosphorylation of the Ser-6 residue by G-kinase presumably weakens the interaction between the DNA-binding amino acids of HMG 14 and the negatively charged phosphate groups of DNA.
利用牛肺中的环磷酸鸟苷依赖性蛋白激酶和大鼠肝脏中的核蛋白激酶II，研究了磷酸化对小牛胸腺HMG 14与单链DNA（ssDNA）亲和力的影响。当被G激酶磷酸化时，HMG 14在0.27M NaCl浓度下从ssDNA柱上洗脱，而天然蛋白在0.30M盐浓度下洗脱。相反，核蛋白激酶II的磷酸化并没有改变HMG 14与ssDNA的解离，因此磷酸化蛋白与天然HMG 14共洗脱。因此，G激酶对Ser-6残基的磷酸化增加了负电荷，可能削弱了HMG 14的DNA结合氨基酸与DNA带负电荷的磷酸基团之间的相互作用。
