{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Connelly KRS"],"funding":["Medical Research Council","Biotechnology and Biological Sciences Research Council"],"pagination":["2136-2146"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5203670"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["162(12)"],"pubmed_abstract":["Salmonella enterica serovar Typhimurium is a Gram-negative bacterium with a flexible respiratory capability. Under anaerobic conditions, S. enterica can utilize a range of terminal electron acceptors, including selenate, to sustain respiratory electron transport. The S. enterica selenate reductase is a membrane-bound enzyme encoded by the ynfEFGH-dmsD operon. The active enzyme is predicted to comprise at least three subunits where YnfE is a molybdenum-containing catalytic subunit. The YnfE protein is synthesized with an N-terminal twin-arginine signal peptide and biosynthesis of the enzyme is coordinated by a signal peptide binding chaperone called DmsD. In this work, the interaction between S. enterica DmsD and the YnfE signal peptide has been studied by chemical crosslinking. These exper"],"journal":["Microbiology (Reading, England)"],"pubmed_title":["Biosynthesis of selenate reductase in Salmonella enterica: critical roles for the signal peptide and DmsD."],"pmcid":["PMC5203670"],"funding_grant_id":["G1100142","BB/D018986/1"],"pubmed_authors":["Stevenson C","Sargent F","Connelly KRS","Kneuper H"],"additional_accession":[]},"is_claimable":false,"name":"Biosynthesis of selenate reductase in Salmonella enterica: critical roles for the signal peptide and DmsD.","description":"Salmonella enterica serovar Typhimurium is a Gram-negative bacterium with a flexible respiratory capability. Under anaerobic conditions, S. enterica can utilize a range of terminal electron acceptors, including selenate, to sustain respiratory electron transport. The S. enterica selenate reductase is a membrane-bound enzyme encoded by the ynfEFGH-dmsD operon. The active enzyme is predicted to comprise at least three subunits where YnfE is a molybdenum-containing catalytic subunit. The YnfE protein is synthesized with an N-terminal twin-arginine signal peptide and biosynthesis of the enzyme is coordinated by a signal peptide binding chaperone called DmsD. In this work, the interaction between S. enterica DmsD and the YnfE signal peptide has been studied by chemical crosslinking. These exper","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Dec","modification":"2025-05-29T20:26:14.785Z","creation":"2025-05-29T20:26:14.785Z"},"accession":"S-EPMC5203670","cross_references":{"pubmed":["27902441"],"doi":["10.1099/mic.0.000381"]}}