Distinguishing functional from structural roles of conserved pore residues during formate translocation by the FocA anion channel.

ABSTRACT: The formate-specific anion channel FocA of Escherichia coli belongs to the superfamily of homopentameric formate-nitrite transporters (FNT). Minimally nine amino acid residues are conserved in the formate translocation pore of each protomer of the pentamer, including a histidine (H209) and a threonine (T91), both of which are crucial for bidirectional formate translocation through the pore. Information regarding in vivo functional or structural roles for the other seven conserved residues is limited, or nonexistent. Here, we conducted an amino acid-exchange analysis of these seven conserved residues. Using an established formate-responsive lacZ-based assay to monitor changes in intracellular formate levels and anaerobic growth rate due to the inhibitory formate analog hypophosphite, we ide

SUBMITTER: Kammel M 

PROVIDER: S-EPMC9380403 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature