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Binding of Glutathione and ppGpp to Stringent Starvation Protein A (SspA)
Taner Duysak,Le Phuong Nguyen,정제훈 대한화학회 2020 Bulletin of the Korean Chemical Society Vol.41 No.9
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 ?M and 75.3?±?4.3 ?M, 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 ?M. This study may provide an insight why relA is required for regulating gene expression by SspA.