In vivo evaluation of the interaction between the Escherichia coli IGP synthase subunits using the Bacterial Two-Hybrid system

ABSTRACT Histidine biosynthesis is one of the most characterized metabolic routes for its antiquity and its central role in cellular metabolism; indeed, it represents a cross-road between nitrogen metabolism and de novo synthesis of purines. This interconnection is due to the activity of imidazole g...

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Bibliographic Details
Published in:FEMS microbiology letters 2020-07, Vol.367 (14), p.1
Main Authors: Chioccioli, Sofia, Bogani, Patrizia, Del Duca, Sara, Castronovo, Lara Mitia, Vassallo, Alberto, Puglia, Anna Maria, Fani, Renato
Format: Article
Language:English
Subjects:
Adenylate cyclase
Biosynthesis
Complex formation
Drug development
E coli
Enzymes
Escherichia coli
Genes
Glutamine
Glutamine amidotransferase
Glycerol
Histidine
Hybrid systems
Imidazole
Metabolism
Microbiology
Nitrogen metabolism
Physiological aspects
Proteins
Purines
Yeasts
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Summary:ABSTRACT Histidine biosynthesis is one of the most characterized metabolic routes for its antiquity and its central role in cellular metabolism; indeed, it represents a cross-road between nitrogen metabolism and de novo synthesis of purines. This interconnection is due to the activity of imidazole glycerol phosphate synthase, a heterodimeric enzyme constituted by the products of two his genes, hisH and hisF, encoding a glutamine amidotransferase and a cyclase, respectively. Despite their interaction was suggested by several in vitro experiments, their in vivo complex formation has not been demonstrated. On the contrary, the analysis of the entire Escherichia coli interactome performed using the yeast two hybrid system did not suggest the in vivo interaction of the two IGP synthase subunits. The aim of this study was to demonstrate the interaction of the two proteins using the Bacterial Adenylate Cyclase Two-Hybrid (BACTH) system. Data obtained demonstrated the in vivo interaction occurring between the proteins encoded by the E. coli hisH and hisF genes; this finding might also open the way to pharmaceutical applications through the design of selective drugs toward this enzyme. In vivo analysis of HisH and HisF protein interaction in E. coli using the BACTH system.
ISSN:1574-6968
0378-1097
1574-6968
DOI:10.1093/femsle/fnaa112