Wei Y F, Morgan J E, Matthews H R
Department of Biological Chemistry, University of California, Davis 95616.
Arch Biochem Biophys. 1989 Feb 1;268(2):546-50. doi: 10.1016/0003-9861(89)90321-4.
Histone H4 is a good substrate in vitro for the protein histidine kinase activity found both in Physarum polycephalum nuclear extracts and in Saccharomyces cerevisiae cell extracts. However, histone H4 in nucleosome core particles is not a substrate for these kinases. Isolated chromatin was also not a substrate for the protein histidine kinase. The results significantly limit possible interpretations of histidine phosphorylation on histone H4 in vivo and provide a new, sharper focus for future work. In addition, a polynucleotide kinase activity was identified in the Physarum extracts.
组蛋白H4在体外是多头绒泡菌核提取物和酿酒酵母细胞提取物中发现的蛋白质组氨酸激酶活性的良好底物。然而，核小体核心颗粒中的组蛋白H4不是这些激酶的底物。分离的染色质也不是蛋白质组氨酸激酶的底物。这些结果显著限制了体内组蛋白H4上组氨酸磷酸化的可能解释，并为未来的工作提供了一个新的、更明确的重点。此外，在多头绒泡菌提取物中鉴定出一种多核苷酸激酶活性。
