Characterization of the Interaction Between the Small Regulatory Peptide SgrT and the EIICBGlc of the Glucose-Phosphotransferase System of E. coli K-12

Metabolites

Anne Kosfeld¹ 

[1] Centre for Pathology and Forensic and Genetic Medicine, Institute for Human Genetics-Hannover Medical School, Carl-Neuberg-Str.1, D-30625 Hannover, Germany

关键词: glucose transporter;    glucose signaling;    PTS;    regulation;    protein–protein interaction;    SgrT;    E. coli K-12;   

DOI  :  10.3390/metabo2040756

来源: mdpi

【 摘 要 】

Escherichia coli is a widely used microorganism in biotechnological processes. An obvious goal for current scientific and technical research in this field is the search for new tools to optimize productivity. Usually glucose is the preferred carbon source in biotechnological applications. In E. coli, glucose is taken up by the phosphoenolpyruvate-dependent glucose phosphotransferase system (PTS). The regulation of the ptsG gene for the glucose transporter is very complex and involves several regulatory proteins. Recently, a novel posttranscriptional regulation system has been identified which consists of a small regulatory RNA SgrS and a small regulatory polypeptide called SgrT. During the accumulation of glucose-6-phosphate or fructose-6-phosphate, SgrS is involved in downregulation of ptsG mRNA stability, whereas SgrT inhibits glucose transport activity by a yet unknown mechanism. The function of SgrS has been studied intensively. In contrast, the knowledge about the function of SgrT is still limited. Therefore, in this paper, we focused our interest on the regulation of glucose transport activity by SgrT. We identified the SgrT target sequence within the glucose transporter and characterized the interaction in great detail. Finally, we suggest a novel experimental approach to regulate artificially carbohydrate uptake in E. coli to minimize metabolic overflow in biotechnological applications.

【 授权许可】

CC BY   
© 2012 by the authors; licensee MDPI, Basel, Switzerland.