ArticleProceedings of the National Academy of Sciences of the United States of America2012
The formate channel FocA exports the products of mixed-acid fermentation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
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- Intrinsic Asymmetry in Weak Acid Transmembrane Transporters.Biomolecules · 2026Review
- Structure of Chlamydomonas reinhardtii LciA guided the engineering of FNT family proteins to gain bicarbonate transport activity.Nature plants · 2026Article
- Specificities of chemosensory receptors in the human gut microbiota.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A pH Fingerprint Assay to Identify Inhibitors of Multiple Validated and Potential Antimalarial Drug Targets.ACS infectious diseases · 2024Article
- Microbial membrane transport proteins and their biotechnological applications.World journal of microbiology & biotechnology · 2024Review
- Formate production is dispensable forInfection and immunity · 2023Article
- Formate Metabolism in Shigella flexneri and Its Effect on HeLa Cells at Different Stages during the Infectious Process.Microbiology spectrum · 2023Article
- Article
- Function Investigations and Applications of Membrane Proteins on Artificial Lipid Membranes.International journal of molecular sciences · 2023Review
- Comparison of ion selectivities of nitrite channel NirC and water channel aquaporin.World journal of microbiology & biotechnology · 2023Article
- Human monocarboxylate transporters accept and relay protons via the bound substrate for selectivity and activity at physiological pH.PNAS nexus · 2023Article
- Evolutionary Overview of Aquaporin Superfamily.Advances in experimental medicine and biology · 2023Article
- The Metabolic Adaptation in Response to Nitrate Is Critical for Actinobacillus pleuropneumoniae Growth and Pathogenicity under the Regulation of NarQ/P.Infection and immunity · 2022Article
- Integrating Genome-Resolved Metagenomics with Trait-Based Process Modeling to Determine Biokinetics of Distinct Nitrifying Communities within Activated Sludge.Environmental science & technology · 2022Article
- The Loss ofMicroorganisms · 2022Article
- Distinguishing functional from structural roles of conserved pore residues during formate translocation by the FocA anion channel.MicrobiologyOpen · 2022Article
- Genes Differentially Expressed by Haemophilus ducreyi during Anaerobic Growth Significantly Overlap Those Differentially Expressed during Experimental Infection of Human Volunteers.Journal of bacteriology · 2022Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Formate is a major metabolite in the anaerobic fermentation of glucose by many enterobacteria. It is translocated across cellular membranes by the pentameric ion channel/transporter FocA that, together with the nitrite channel NirC, forms the formate/nitrite transporter (FNT) family of membrane transport proteins. Here we have carried out an electrophysiological analysis of FocA from Salmonella typhimurium to characterize the channel properties and assess its specificity toward formate and other possible permeating ions. Single-channel currents for formate, hypophosphite and nitrite revealed two mechanistically distinct modes of gating that reflect different types of structural rearrangements in the transport channel of each FocA protomer. Moreover, FocA did not conduct cations or divalent anions, but the chloride anion was identified as further transported species, along with acetate, lactate and pyruvate. Formate, acetate and lactate are major end products of anaerobic mixed-acid fermentation, the pathway where FocA is predominantly required, so that this channel is ideally adapted to act as a multifunctional export protein to prevent their intracellular accumulation. Because of the high degree of conservation in the residues forming the transport channel among FNT family members, the flexibility in conducting multiple molecules is most likely a general feature of these proteins.
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