蛋白激酶亚基在真核生物基因表达调控中的作用。

D Schlichter, H Miller, W D Wicks
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引用次数: 0

摘要

cAMP的转录调控作用已被证明适用于几种真核生物基因;然而,所涉及的蛋白激酶亚基的身份一直是争论的来源。基于与原核生物camp结合分解代谢激活蛋白的同源性,最近有一种假说认为调控蛋白RII是中介。然而,目前关于微注射激酶亚基作用的证据表明,催化亚基是活性因子。此外,分解代谢激活蛋白与RII之间的同源性很难与其所提出的介导作用相协调。我们提出了另一种假说,即除了RII以外,还有一种磷酸化蛋白可能介导cAMP对真核基因表达的影响。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
On the role of protein kinase subunits in the control of eukaryotic gene expression.

Transcriptional regulation by cAMP has been demonstrated for several eukaryotic genes; however, the identity of the protein kinase subunit involved has been a source of debate. Based on homologies with the procaryotic cAMP-binding catabolite activator protein, a recent hypothesis has invoked the regulatory protein RII as the mediator. The evidence currently available on the effects of microinjected kinase subunits suggests, however, that the catalytic subunit is the active factor. Moreover, the proposed homologies between the catabolite activator protein and RII are difficult to reconcile with its proposed mediatory role. We suggest as an alternative hypothesis that a phosphoprotein other than RII may mediate the effects of cAMP on eukaryotic gene expression.

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