Binding of Glutathione and ppGpp to Stringent Starvation Protein A (SspA),Bulletin of the Korean Chemical Society

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Binding of Glutathione and ppGpp to Stringent Starvation Protein A (SspA)
Bulletin of the Korean Chemical Society ( IF 2.3 ) Pub Date : 2020-08-10 , DOI: 10.1002/bkcs.12089
Taner Duysak ₁ , Le Phuong Nguyen ₁ , Che‐Hun Jung _{1,

2}

Affiliation

Stringent starvation protein A (SspA) is a glutathione S‐transferase homolog. In this study, his₆‐tagged SspA from Escherischia coli has been cloned and over‐expressed. SspA binds glutathione and 1‐chloro‐2,4‐dinitrobenzene, the substrates for glutathione S‐transferases, with the dissociation constants as 225.0 ± 34.4 μM and 75.3 ± 4.3 μM, respectively. This observation is contradictory to the previous report that SspA, lacking glutathione S‐transferase activity, does not bind glutathione. It has been reported that SspA is an RNA polymerase‐associated transcription factor and that a functional relA gene is required for SspA to affect gene expression. A function of relA is to synthesize ppGpp, a global regulator in replication, transcription, and translation. This study shows for the first time that SspA binds ppGpp with the dissociation of constants of 109.1 ± 7.2 μM. This study may provide an insight why relA is required for regulating gene expression by SspA.

中文翻译：

谷胱甘肽和ppGpp与严格饥饿蛋白A（SspA）的结合

严格的饥饿蛋白A（SspA）是谷胱甘肽S-转移酶的同源物。在这项研究中，他的₆标记的SspA来自大肠杆菌已被克隆并过表达。SspA结合谷胱甘肽S-转移酶的底物谷胱甘肽和1-氯-2,4-二硝基苯，解离常数分别为225.0±34.4μM和75.3±4.3μM。该观察结果与以前的报道相矛盾，即缺乏谷胱甘肽S-转移酶活性的SspA不结合谷胱甘肽。据报道，SspA是与RNA聚合酶相关的转录因子，SspA影响基因表达需要功能性relA基因。relA的功能是合成ppGpp，ppGpp是复制，转录和翻译中的全局调节子。这项研究首次显示SspA以109.1±7.2μM的常数解离结合ppGpp。这项研究可能提供了一个洞察力，为什么relA才能通过SspA调节基因表达。

更新日期：2020-09-20

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