{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bruna RE"],"funding":["NIAID NIH HHS","HHS | NIH | National Institute of Allergy and Infectious Diseases"],"pagination":["e2021370118"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7980370"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["118(11)"],"pubmed_abstract":["Phosphorus (P) is an essential component of core biological molecules. In bacteria, P is acquired mainly as inorganic orthophosphate (Pi) and assimilated into adenosine triphosphate (ATP) in the cytoplasm. Although P is essential, excess cytosolic Pi hinders growth. We now report that bacteria limit Pi uptake to avoid disruption of Mg<sup>2+</sup>-dependent processes that result, in part, from Mg<sup>2+</sup> chelation by ATP. We establish that the MgtC protein inhibits uptake of the ATP precursor Pi when <i>Salmonella enterica</i> serovar Typhimurium experiences cytoplasmic Mg<sup>2+</sup> starvation. This response prevents ATP accumulation and overproduction of ribosomal RNA that together ultimately hinder bacterial growth and result in loss of viability. Even when cytoplasmic Mg<sup>2+<"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Limitation of phosphate assimilation maintains cytoplasmic magnesium homeostasis."],"pmcid":["PMC7980370"],"funding_grant_id":["AI148774","R21 AI148774","R01 AI049561"],"pubmed_authors":["Pontes MH","Kendra CG","Bruna RE","Groisman EA"],"additional_accession":[]},"is_claimable":false,"name":"Limitation of phosphate assimilation maintains cytoplasmic magnesium homeostasis.","description":"Phosphorus (P) is an essential component of core biological molecules. In bacteria, P is acquired mainly as inorganic orthophosphate (Pi) and assimilated into adenosine triphosphate (ATP) in the cytoplasm. Although P is essential, excess cytosolic Pi hinders growth. We now report that bacteria limit Pi uptake to avoid disruption of Mg<sup>2+</sup>-dependent processes that result, in part, from Mg<sup>2+</sup> chelation by ATP. We establish that the MgtC protein inhibits uptake of the ATP precursor Pi when <i>Salmonella enterica</i> serovar Typhimurium experiences cytoplasmic Mg<sup>2+</sup> starvation. This response prevents ATP accumulation and overproduction of ribosomal RNA that together ultimately hinder bacterial growth and result in loss of viability. Even when cytoplasmic Mg<sup>2+<","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Mar","modification":"2025-04-04T22:01:03.946Z","creation":"2025-04-04T22:01:03.946Z"},"accession":"S-EPMC7980370","cross_references":{"pubmed":["33707210"],"doi":["10.1073/pnas.2021370118"]}}