Nesterova M V, Glukhov A I, Aprikian A G, Severin E S
Biokhimiia. 1987 Jul;52(7):1150-3.
The phosphorylation of nuclear proteins of porcine brain cAMP-dependent protein kinase was studied. Some nuclear proteins after extraction from the nuclei served as substrates for protein kinase. Lysine-rich histones H1, H2a and H2b were found to accept phosphate during chromatin phosphorylation by cAMP-dependent protein kinase. Phosphorylation of intact nuclei revealed that in such a system only histone H1 is a substrate for cAMP-dependent protein kinase. In the presence of DNA the histones are phosphorylated by cAMP-dependent protein kinase in a different manner. It was concluded that DNA can determine the accessibility of protein substrates for the catalytic subunit of cAMP-dependent protein kinase.
对猪脑cAMP依赖性蛋白激酶的核蛋白磷酸化进行了研究。从细胞核中提取后，一些核蛋白作为蛋白激酶的底物。发现富含赖氨酸的组蛋白H1、H2a和H2b在cAMP依赖性蛋白激酶介导的染色质磷酸化过程中接受磷酸基团。完整细胞核的磷酸化表明，在这样的系统中，只有组蛋白H1是cAMP依赖性蛋白激酶的底物。在DNA存在的情况下，组蛋白被cAMP依赖性蛋白激酶以不同方式磷酸化。得出的结论是，DNA可以决定cAMP依赖性蛋白激酶催化亚基对蛋白质底物的可及性。
