大肠杆菌中硝酸还原酶合成的定位与调控
Localization and regulation of synthesis of nitrate reductase in Escherichia coli.
作者信息
Showe M K, DeMoss J A
出版信息
J Bacteriol. 1968 Apr;95(4):1305-13. doi: 10.1128/jb.95.4.1305-1313.1968.
Abstract
The nitrate reductase of Escherichia coli K-12 was localized in a particulate fraction of the cell and it sedimented as if it were bound to a large substructure that is subject to fragmentation during cell disruption procedures. Soluble enzyme, exhibiting a homogenous profile in sucrose gradients, was released from this fraction by an alkaline-heat treatment. Less than 1.5% of total active nitrate reductase apparently occurred in this soluble form during the course of formation of the particulate enzyme. Enzyme synthesis was repressed by aeration in the presence or absence of nitrate. Under anaerobic conditions, nitrate reductase was synthesized at a rate that could be increased 20-fold by the addition of nitrate. When enzyme synthesis was initiated by induction with nitrate or anaerobiosis, biphasic kinetics were obtained. We interpreted the results as evidence for the existence of a redox-sensitive repressor which mediates nitrate reductase regulation.
摘要
大肠杆菌K-12的硝酸还原酶定位于细胞的颗粒部分，其沉降方式表明它似乎与一个大的亚结构结合，该亚结构在细胞破碎过程中会发生断裂。在蔗糖梯度中呈现均匀分布的可溶性酶，通过碱热处理从该部分释放出来。在颗粒酶形成过程中，总活性硝酸还原酶中显然只有不到1.5%以这种可溶性形式存在。无论有无硝酸盐，通气都会抑制酶的合成。在厌氧条件下，硝酸还原酶的合成速率可通过添加硝酸盐提高20倍。当通过硝酸盐诱导或厌氧诱导启动酶合成时，会获得双相动力学。我们将这些结果解释为存在一种介导硝酸还原酶调节的氧化还原敏感阻遏物的证据。
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