Polyamine-activated protein kinase reaction from nuclei and nucleoli of Physarum polycephalum which phosphorylates a unique Mr 70 000 nonhistone protein.
Polyamine-activated protein kinase reaction from nuclei and nucleoli of Physarum polycephalum which phosphorylates a unique Mr 70 000 nonhistone protein.
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来自多头绒泡菌的细胞核和核仁的多胺激活蛋白激酶反应，磷酸化独特的 Mr 70 000 非组蛋白。
DOI：
10.1021/bi00512a025
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发表时间：
1981
期刊：
影响因子：
2.9
通讯作者：
Kuehn,GD
中科院分区：
文献类型：
--
作者：
Daniels,GR;Atmar,VJ;Kuehn,GD
摘要：描述了从多头绒泡菌的细胞核和核仁中检测和纯化蛋白激酶的方法，该蛋白激酶在多胺依赖的反应中催化磷酸从[-32]转移到唯一的非组蛋白MT 70000。多胺、亚精胺和精胺对非组蛋白蛋白的酶促磷酸化作用明显增强，有时可达60倍以上。这种独特的多胺依赖反应定位于核仁的rDNA微染色体上。多胺依赖的蛋白激酶首先用分离的非组蛋白酸性蛋白溶解部分纯化，然后用磷酸纤维素层析法从至少六种其他蛋白激酶中分离出催化组分。
Gary R. Daniels, Valerie J. Atmar, and Glenn D. Kuehn* abstract: Methods are described for the detection and pu-rification of a protein kinase from nuclei and nucleoli of Physarum polycephalum which catalyzed transfer of phos-phate from [-32] to a unique nonhistone protein of MT 70000 in a reaction that was polyamine dependent. Enzymatic phosphorylation of the nonhistone protein by the purified protein kinase was stimulated greatly, at times more than 60-fold, by the polyamines spermidine and spermine. This unique polyamine-dependent reaction was localized on the rDNA minichromosome of the nucleolus. The polyamine-dependent protein kinase, which was first partially purified with the acidic nonhistone proteinfraction from isolated nu-cleoli, was resolved from at least six other protein kinases by phosphocellulose chromatography into a catalytic component