The ArcB Sensor Kinase of Escherichia coli Autophosphorylates by an Intramolecular Reaction
The ArcB Sensor Kinase of Escherichia coli Autophosphorylates by an Intramolecular Reaction
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DOI：
10.1128/jb.01401-09
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发表时间：
2010-03-15
影响因子：
3.2
通讯作者：
Georgellis, Dimitris
中科院分区：
文献类型：
--
作者：
Pena-Sandoval, Gabriela R.;Georgellis, Dimitris
Arc 双组分系统由 ArcB 传感器激酶和 ArcA 响应调节器组成，可根据生长的呼吸条件调节众多基因的表达。 ArcB 是一种三联组氨酸激酶，其活性通过参与分子间二硫键形成的两个位于胞质溶胶的氧化还原活性半胱氨酸残基的氧化来调节。在这里，我们展示了 ArcB 通过分子内反应进行自磷酸化，该反应不同于通常设想的同二聚组氨酸激酶的分子间自磷酸化。
The Arc two-component system, comprising the ArcB sensor kinase and the ArcA response regulator, modulates the expression of numerous genes in response to the respiratory conditions of growth. ArcB is a tripartite histidine kinase whose activity is regulated by the oxidation of two cytosol-located redox-active cysteine residues that participate in intermolecular disulfide bond formation. Here we show that ArcB auto-phosphorylates through an intramolecular reaction which diverges from the usually envisaged intermolecular autophosphorylation of homodimeric histidine kinases.