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首页> 外文期刊>Journal of Molecular Biology >Kinetic partitioning between alternative protein-protein interactions controls a transcriptional switch.
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Kinetic partitioning between alternative protein-protein interactions controls a transcriptional switch.

机译：交替的蛋白质-蛋白质相互作用之间的动力学分配控制转录开关。

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摘要

Proteins can perform completely distinct functions in response to the particular partners that they bind to. Consequently, determination of the mechanism of functional regulation in such systems requires elucidation of the mechanism switching between binding partners. The central protein of the Escherichia coli biotin regulatory system, BirA, switches between its function as a metabolic enzyme or a transcriptional repressor in response to binding either the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase or a second BirA monomer. These two protein-protein interactions are structurally mutually exclusive. The results of earlier studies suggest that the system is regulated by kinetic partitioning between the two protein-protein interactions. In this work, sedimentation velocity was employed to monitor the partitioning directly. The results indicate similar equilibrium parameters governing formation of the two protein-protein interactions. Kinetic analysis of the sedimentation velocity data indicated that holoBirA dimerization is governed by very slow forward and reverse rate constants. The slow kinetics of holoBirA dimerization combined with fluctuations in the intracellular apoBCCP pool are critical determinants in partitioning BirA between its distinct biological functions.
机译：蛋白质可以响应与其结合的特定配偶体而执行完全不同的功能。因此，在这种系统中确定功能调节的机制需要阐明在结合伴侣之间切换的机制。大肠杆菌生物素调节系统的中心蛋白BirA响应于结合乙酰辅酶A羧化酶的生物素羧基载体蛋白亚基或第二种BirA单体，在其作为代谢酶或转录阻遏物的功能之间切换。这两种蛋白质-蛋白质相互作用在结构上是互斥的。早期研究的结果表明，该系统受两种蛋白质-蛋白质相互作用之间的动力学分配调节。在这项工作中，采用沉降速度直接监测分区。结果表明，相似的平衡参数控制着两种蛋白质-蛋白质相互作用的形成。沉降速度数据的动力学分析表明，holoBirA二聚化受非常慢的正向和反向速率常数控制。 holoBirA二聚化的缓慢动力学以及细胞内apoBCCP库中的波动是在BirA在其独特的生物学功能之间进行分配的关键决定因素。

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