Glucose Transport through N-Acetylgalactosamine Phosphotransferase System in Escherichia coli C Strain.

ABSTRACT: When ptsG, a glucose-specific phosphotransferase system (PTS) component, is deleted in Escherichia coli, growth can be severely poor because of the lack of efficient glucose transport. We discovered a new PTS transport system that could transport glucose through the growth-coupled experimental evolution of ptsG-deficient E. coli C strain under anaerobic conditions. Genome sequencing revealed mutations in agaR, which encodes a repressor of N-acetylgalactosamine (Aga) PTS expression in evolved progeny strains. RT-qPCR analysis showed that the expression of Aga PTS gene increased because of the loss-of-function of agaR. We confirmed the efficient Aga PTS-mediated glucose uptake by genetic complementation and anaerobic fermentation. We discussed

SUBMITTER: Kim HJ 

PROVIDER: S-EPMC9628945 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature