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首页> 外文期刊>Journal of Molecular Biology >Protein:Protein interactions in control of a transcriptional switch
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Protein:Protein interactions in control of a transcriptional switch

机译：蛋白质：蛋白质相互作用控制转录开关

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摘要

Protein partner exchange plays a key role in regulating many biological switches. Although widespread, the mechanisms dictating protein partner identity and, therefore, the outcome of a switch have been determined for a limited number of systems. The Escherichia coli protein BirA undergoes a switch between posttranslational biotin attachment and transcription repression in response to cellular biotin demand. Moreover, the functional switch reflects formation of alternative mutually exclusive protein:protein interactions by BirA. Previous studies provided a set of alanine-substituted BirA variants with altered kinetic and equilibrium parameters of forming these interactions. In this work, DNase I footprinting measurements were employed to investigate the consequences of these altered properties for the outcome of the BirA functional switch. The results support a mechanism in which BirA availability for DNA binding and, therefore, transcription repression is controlled by the rate of the competing protein:protein interaction. However, occupancy of the transcriptional regulatory site on DNA by BirA is exquisitely tuned by the equilibrium constant governing its homodimerization.
机译：蛋白质伴侣交换在调节许多生物开关中起关键作用。尽管很普遍，但已经为有限数量的系统确定了决定蛋白质伴侣身份以及因此决定转换结果的机制。大肠杆菌蛋白BirA在翻译后生物素附着和转录抑制之间进行切换，以响应细胞对生物素的需求。此外，功能转换反映了BirA形成互斥的互斥蛋白质：蛋白质相互作用。先前的研究提供了一组丙氨酸取代的BirA变体，这些变体具有形成这些相互作用的动力学和平衡参数。在这项工作中，使用DNase I足迹测量来研究这些改变的特性对BirA功能开关的结果的影响。结果支持了一种机制，其中BirA可用于DNA结合，因此，转录抑制受竞争性蛋白质：蛋白质相互作用的速率控制。但是，BirA对DNA转录调控位点的占据受到控制其同型二聚体的平衡常数的调节。

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