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首页> 外文期刊>Journal of Molecular Biology >Characterizing Lysine Acetylation of Isocitrate Dehydrogenase in Escherichia coli
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Characterizing Lysine Acetylation of Isocitrate Dehydrogenase in Escherichia coli

机译：在大肠杆菌中表征赖氨酸乙酰化酶乙酰化酶

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摘要

The Escherichia coli isocitrate dehydrogenase (ICDH) is one of the tricarboxylic acid cycle enzymes, playing key roles in energy production and carbon flux regulation. E. coli ICDH was the first bacterial enzyme shown to be regulated by reversible phosphorylation. However, the effect of lysine acetylation on E. coli ICDH, which has no sequence similarity with its counterparts in eukaryotes, is still unclear. Based on previous studies of E. coli acetylome and ICDH crystal structures, eight lysine residues were selected for mutational and kinetic analyses. They were replaced with acetyllysine by the genetic code expansion strategy or substituted with glutamine as a classic approach. Although acetylation decreased the overall ICDH activity, its effects were different site by site. Deacetylation tests demonstrated that the CobB deacetylase could deacetylate ICDH both in vivo and in vitro, but CobB was only specific for lysine residues at the protein surface. On the other hand, ICDH could be acetylated by acetyl-phosphate chemically in vitro. And in vivo acetylation tests indicated that the acetylation level of ICDH was correlated with the amounts of intracellular acetyl-phosphate. This study nicely complements previous proteomic studies to provide direct biochemical evidence for ICDH acetylation. (C) 2018 Elsevier Ltd. All rights reserved.
机译：大肠杆菌同源硝酸脱氢酶（ICDH）是三羧酸循环酶之一，在能量产生和碳通量调节中发挥关键作用。大肠杆菌ICDH是第一种通过可逆磷酸化调节的第一种细菌酶。然而，赖氨酸乙酰化对大肠杆菌ICDH的影响，其与真核生物中的对应物没有序列相似性，仍然不清楚。基于先前的大肠杆菌乙酰物和ICDH晶体结构的研究，选择了八个赖氨酸残基用于突变和动力学分析。通过遗传码扩张策略用乙酰覆盖物替换，或者用谷氨酰胺作为经典方法取代。虽然乙酰化降低了整体ICDH活性，但其效果是通过地点的不同部位。脱乙酰化试验证明COBB脱乙酰酶可以在体内和体外脱乙酰酯，但COBB仅对蛋白质表面的赖氨酸残基特异。另一方面，ICDH可以通过在体外化学上的乙酰磷酸酯乙酰化。并且在体内乙酰化试验表明，ICDH的乙酰化水平与细胞内乙酰磷酸酯的量相关。这项研究很好地补充了以前的蛋白质组学研究，以提供ICDH乙酰化的直接生化证据。 （c）2018年elestvier有限公司保留所有权利。

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