ArticleJournal of molecular biology2014
Pyruvate formate-lyase interacts directly with the formate channel FocA to regulate formate translocation.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 58 citations in OpenAlex.
- Nature's Anaerobic Toolkit: Glycyl Radical Enzymes and Their Expanding Functional and Mechanistic Diversity.Biochemistry · 2026Review
- Phosphate-mobilizing bacterial community structure and mobilization mechanisms in tobacco rhizosphere.Current research in microbial sciences · 2026Article
- Conserved hydrophilic checkpoints tune FocA-mediated formate:HNature communications · 2025Article
- How FocA facilitates fermentation and respiration of formate byJournal of bacteriology · 2025Review
- Formate production is dispensable forInfection and immunity · 2023Article
- The Loss ofMicroorganisms · 2022Article
- Distinguishing functional from structural roles of conserved pore residues during formate translocation by the FocA anion channel.MicrobiologyOpen · 2022Article
- The Autonomous Glycyl Radical Protein GrcA Restores Activity to Inactive Full-Length Pyruvate Formate-LyaseJournal of bacteriology · 2022Article
- Hydrogen production in the presence of oxygen byMicrobiology (Reading, England) · 2022Article
- A single amino acid exchange converts FocA into a unidirectional efflux channel for formate.Microbiology (Reading, England) · 2022Article
- Pseudo-Symmetric Assembly of Protodomains as a Common Denominator in the Evolution of Polytopic Helical Membrane Proteins.Journal of molecular evolution · 2020Article
- Energy-converting hydrogenases: the link between HCellular and molecular life sciences : CMLS · 2020Review
- Is the E. coli Homolog of the Formate/Nitrite Transporter Family an Anion Channel? A Computational Study.Biophysical journal · 2020Article
- Article
- Formate PromotesmBio · 2018Article
- Integrating Cross-Linking Experiments with Ab Initio Protein-Protein Docking.Journal of molecular biology · 2018Article
- Energetics and mechanism of anion permeation across formate-nitrite transporters.Scientific reports · 2017Article
- The C-terminal Six Amino Acids of the FNT Channel FocA Are Required for Formate Translocation But Not Homopentamer Integrity.Frontiers in microbiology · 2017Article
- Exploring the directionality of Escherichia coli formate hydrogenlyase: a membrane-bound enzyme capable of fixing carbon dioxide to organic acid.MicrobiologyOpen · 2016Article
- Anaerobic Formate and Hydrogen Metabolism.EcoSal Plus · 2016Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
The FNT (formate-nitrite transporters) form a superfamily of pentameric membrane channels that translocate monovalent anions across biological membranes. FocA (formate channel A) translocates formate bidirectionally but the mechanism underlying how translocation of formate is controlled and what governs substrate specificity remains unclear. Here we demonstrate that the normally soluble dimeric enzyme pyruvate formate-lyase (PflB), which is responsible for intracellular formate generation in enterobacteria and other microbes, interacts specifically with FocA. Association of PflB with the cytoplasmic membrane was shown to be FocA dependent and purified, Strep-tagged FocA specifically retrieved PflB from Escherichia coli crude extracts. Using a bacterial two-hybrid system, it could be shown that the N-terminus of FocA and the central domain of PflB were involved in the interaction. This finding was confirmed by chemical cross-linking experiments. Using constraints imposed by the amino acid residues identified in the cross-linking study, we provide for the first time a model for the FocA-PflB complex. The model suggests that the N-terminus of FocA is important for interaction with PflB. An in vivo assay developed to monitor changes in formate levels in the cytoplasm revealed the importance of the interaction with PflB for optimal translocation of formate by FocA. This system represents a paradigm for the control of activity of FNT channel proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.