3':5'-环磷酸腺苷作为大肠杆菌中分解代谢物阻遏的介质。
Adenosine 3':5'-cyclic monophosphate as mediator of catabolite repression in Escherichia coli.
作者信息
Epstein W, Rothman-Denes L B, Hesse J
出版信息
Proc Natl Acad Sci U S A. 1975 Jun;72(6):2300-4. doi: 10.1073/pnas.72.6.2300.
Abstract
Measurements of intracellular adenosine 3':5'-cyclic monophosphate (cAMP) concentrations in E. coli under a variety of conditions show that levels of this nucleotide are well correlated with the rate of synthesis of beta-galactosidase (beta-D-galactoside galactohydrolase, EC 3.2.1.23) in both catabolite repression and transient repression. These results, combined with extensive genetic and in vitro studies from a number of laboratories on the role of cAMP in E. coli, provide strong support for the concept that intracellular cAMP levels mediate the effects of catabolite and transient repression on rates on enzyme synthesis. Under all conditions studied, excretion can be described by a single rate constant, 2.1 min-1 at 37 degrees, indicating that intracellular levels cannot be regulated by alterations in the rate of cAMP excretion. Our data are fully consistent with the idea that carbon sources control intracellular cAMP levels by effects on its synthesis.
摘要
在各种条件下对大肠杆菌细胞内3':5'-环磷酸腺苷（cAMP）浓度的测量表明，在分解代谢物阻遏和瞬时阻遏中，这种核苷酸的水平与β-半乳糖苷酶（β-D-半乳糖苷半乳糖水解酶，EC 3.2.1.23）的合成速率密切相关。这些结果，再结合多个实验室对cAMP在大肠杆菌中的作用进行的广泛遗传学和体外研究，为细胞内cAMP水平介导分解代谢物和瞬时阻遏对酶合成速率的影响这一概念提供了有力支持。在所有研究条件下，排泄可用一个单一的速率常数来描述，在37摄氏度时为2.1分钟-1，这表明细胞内水平不能通过cAMP排泄速率的改变来调节。我们的数据完全符合碳源通过影响其合成来控制细胞内cAMP水平这一观点。
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