Detection of a mammalian histone H4 kinase that has yeast histidine kinase-like enzymic activity

被引:39
作者
Besant, PG [1 ]
Attwood, PV [1 ]
机构
[1] Univ Western Australia, Dept Biochem, Nedlands, WA 6907, Australia
基金
澳大利亚研究理事会;
关键词
histidine kinase; phosphohistidine; histone H4; in-gel kinase assay; phosphoamino acid analysis;
D O I
10.1016/S1357-2725(99)00119-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A well characterized histidine kinase purified from yeast has been shown to phosphorylate histone H4 on a histidine residue. This enzyme is unlike the two-component histidine kinases predominantly found in prokaryotes. Until now, a histidine kinase similar to this yeast enzyme has not been purified from a mammalian source.By using a purification scheme similar to that used to purify the yeast histidine kinase, a protein fraction with histone H4 kinase activity has been isolated from porcine thymus. The yeast histidine kinase was shown to be detectable using an in-gel kinase assay system and using this system, four major bands of histone H4 kinase activity were apparent in the porcine thymus preparation. Through the use of immunoprecipitation, alkaline hydrolysis and subsequent phosphoamino acid analysis it has been demonstrated that this partially purified kinase fraction is capable of phosphorylating histone H4 on histidine. In conclusion, an preparation has been made from porcine thymus that contains histone H4 kinase activity and at least one of the kinases present in this preparation is a histidine kinase. (C) 2000 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:243 / 253
页数:11
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