Coinfection of insect cells with recombinant baculovirus expressing pp60v-src results in the activation of a serine-specific protein kinase pp90rsk.

Coinfection of insect cells with recombinant baculovirus expressing pp60v-src results in the activation of a serine-specific protein kinase pp90rsk.
复制标题

昆虫细胞与表达 pp60v-src 的重组杆状病毒共感染会导致丝氨酸特异性蛋白激酶 pp90rsk 的激活。

DOI:
10.1073/pnas.87.7.2685
复制
发表时间:
1990
影响因子:
11.1
通讯作者:
Erikson,RL
Erikson,RL
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Vik,TA;Sweet,LJ;Erikson,RL

文献摘要

被引文献

相似文献

构建了一种重组杆状病毒,用于在昆虫细胞中生产丝氨酸特异性蛋白激酶pp90rsk(其中rsk为核糖体S6激酶)。与与v-src致癌基因产物pp60v-src共同产生的酶相比,在感染细胞中表达的爪蟾pp90rsk酶活性几乎无法检测到。转化基因产物pp60v-src非常有效地激活了pp90rsk,而c-src和豆芽糖酰化阴性非转化病毒NY315的产物效果明显较差。只有一小部分pp90rsk被激活,并且可以通过离子交换色谱法从未激活的蛋白中分离出部分pp90rsk。与未激活的形式相比,激活的酶磷酸化核糖体蛋白S6的能力增加了约4000倍。酶活性的增强似乎是由于pp90rsk的磷酸化。
A recombinant baculovirus was constructed for the production of the serine-specific protein kinase, pp90rsk (where rsk is ribosomal S6 kinase), in insect cells. The Xenopus pp90rsk expressed in the infected cells had nearly undetectable enzyme activity in contrast to the same enzyme coproduced with the v-src oncogene product pp60v-src. The transforming gene product pp60v-src very effectively activated pp90rsk, whereas the products of c-src and the myristoylation-minus nontransforming virus NY315 were markedly less effective. Only a fraction of the total pp90rsk population was activated, and it could be partially separated from unactivated protein by ion-exchange chromatography. When compared to the unactivated form, the activated enzyme displayed about a 4000-fold increase in the capacity to phosphorylate the ribosomal protein S6. The enhanced enzymatic activity appeared to be due to phosphorylation of pp90rsk.