{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Steingard CH"],"funding":["HHS | National Institutes of Health","NIGMS NIH HHS"],"pagination":["e0002223"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10127796"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["205(4)"],"pubmed_abstract":["The ferric uptake regulator (Fur) protein is the founding member of the FUR superfamily of metalloregulatory proteins that control metal homeostasis in bacteria. FUR proteins regulate metal homeostasis in response to the binding of iron (Fur), zinc (Zur), manganese (Mur), or nickel (Nur). FUR family proteins are generally dimers in solution, but the DNA-bound complex can involve a single dimer, a dimer-of-dimers, or an extended array of bound protein. Elevated FUR levels due to changes in cell physiology increase DNA occupancy and may also kinetically facilitate protein dissociation. Interactions between FUR proteins and other regulators are commonplace, often including cooperative and competitive DNA-binding interactions within the regulatory region. Further, there are many emerging examp"],"journal":["Journal of bacteriology"],"pubmed_title":["Meddling with Metal Sensors: Fur-Family Proteins as Signaling Hubs."],"pmcid":["PMC10127796"],"funding_grant_id":["R35 GM122461","R35GM122461"],"pubmed_authors":["Steingard CH","Helmann JD"],"additional_accession":[]},"is_claimable":false,"name":"Meddling with Metal Sensors: Fur-Family Proteins as Signaling Hubs.","description":"The ferric uptake regulator (Fur) protein is the founding member of the FUR superfamily of metalloregulatory proteins that control metal homeostasis in bacteria. FUR proteins regulate metal homeostasis in response to the binding of iron (Fur), zinc (Zur), manganese (Mur), or nickel (Nur). FUR family proteins are generally dimers in solution, but the DNA-bound complex can involve a single dimer, a dimer-of-dimers, or an extended array of bound protein. Elevated FUR levels due to changes in cell physiology increase DNA occupancy and may also kinetically facilitate protein dissociation. Interactions between FUR proteins and other regulators are commonplace, often including cooperative and competitive DNA-binding interactions within the regulatory region. Further, there are many emerging examp","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Apr","modification":"2025-04-19T23:51:27.611Z","creation":"2025-04-19T23:51:27.611Z"},"accession":"S-EPMC10127796","cross_references":{"pubmed":["37010421"],"doi":["10.1128/jb.00022-23"]}}