Nuclear matrix: a cell-cycle-dependent site of increased intranuclear protein phosphorylation.
Nuclear matrix: a cell-cycle-dependent site of increased intranuclear protein phosphorylation.
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核基质：核内蛋白质磷酸化增加的细胞周期依赖性位点。
DOI：
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发表时间：
1983
期刊：
影响因子：
--
通讯作者：
Lon D. Hodge
中科院分区：
文献类型：
--
作者：
Sally M. Henry;Lon D. Hodge
有证据表明，核基质是一个细胞周期依赖性的网站增加核内蛋白磷酸化。放射性磷酸盐（32 P）的掺入在有丝分裂前（G2）期最高，在有丝分裂后（G1）期低40-50%。对于总基质蛋白和分子量范围从大于200 kDa至19 kDa的几种单个多肽都观察到了这一点。当基质从正磷酸盐标记的完整细胞中分离时，以及当基质被分离然后在蛋白激酶反应混合物中体外孵育时，可以证明这种现象。分离的基质在体内模拟事件的能力表明在该分离的核部分中存在内源性蛋白磷酸激酶活性和生理底物。当确定氨基酸磷酸化位点时，获得了这种模仿的进一步证据。磷酸丝氨酸是在体外和体内标记的基质中最丰富的磷酸氨基酸，尽管也存在磷酸苏氨酸和磷酸酪氨酸。根据几条数据，内源性基质活性似乎是由于多种蛋白磷酸激酶。由于最大磷酸化与有丝分裂前同时发生，因此磷蛋白可能在有丝分裂事件中发挥作用。这些观察结果扩展和扩大了这一部分的核结构/功能关系的研究，特别是在有丝分裂时的应用。
Evidence is presented that the nuclear matrix is a cell-cycle-dependent site of increased intranuclear protein phosphorylation. The incorporation of radioactive phosphate (32P) is highest during the premitotic (G2) phase and 40-50% less in the postmitotic phase (G1). This is observed for both total matrix protein and for several individual polypeptides ranging in molecular mass from greater than 200 kDa to 19 kDa. The phenomenon can be demonstrated when the matrix is isolated from orthophosphate-labeled intact cells, as well as when the matrix is isolated and then incubated in vitro in a protein kinase reaction mixture. The ability of the isolated matrix to mimic the events in vivo indicates the presence of endogenous protein phosphokinase activity and physiological substrates in this isolated nuclear fraction. Further evidence for such mimicry was obtained when amino acid phosphorylation sites were determined. Phosphoserine is the most abundant phosphoamino acid in the matrix labelled both in vitro and in vivo, although phosphothreonine and phosphotyrosine are also present. On the basis of several pieces of data, the endogenous matrix activity appears to be due to multiple protein phosphokinases. Since the maximum phosphorylation coincides with premitosis, the phosphoproteins may play a role in mitotic events. These observations extend and expand the application of this fraction to the study of nuclear structure/function relationships, particularly at the time of mitosis.
有丝分裂组蛋白H1激酶激活机制的研究。
DOI：
10.1016/0006-291x(80)91625-3
发表时间：
1980
影响因子：
3.1
作者：
Zeilig,CE;Langan,TA
通讯作者：
Langan,TA
cAMP 依赖性蛋白激酶 I 调节亚基中的链间二硫键。
DOI：
--
发表时间：
1982
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Zick,SK;Taylor,SS
通讯作者：
Taylor,SS