Biosynthesis of selenate reductase in Salmonella enterica: critical roles for the signal peptide and DmsD

Katherine R. S. Connelly, Calum Stevenson, Holger Kneuper, Frank Sargent (Lead / Corresponding author)

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Salmonella enterica serovar Typhimurium is a Gram negative bacterium with a flexible respiratory capability. Under anaerobic conditions, S. enterica can utilise a range of terminal electron acceptors to sustain respiratory electron transport chains, including the potentially toxic compound selenate. 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 molybdenumcontaining catalytic subunit. The YnfE protein is synthesised with an N-terminal twinarginine signal peptide and biosynthesis of the enzyme is co-ordinated by a signalpeptide-binding chaperone called DmsD. In this work, the interaction between DmsD and the YnfE signal peptide has been studied by chemical crosslinking. These experiments were complemented by genetic approaches, which identified the DmsD binding epitope within the YnfE signal peptide. YnfE signal peptide residues L24 and A28 were shown to be important for assembly of an active selenate reductase. Conversely, a random genetic screen identified the DmsD V16 residue as being important for signal peptide recognition and selenate reductase assembly.
Original languageEnglish
Pages (from-to)2136-2146
Number of pages11
Issue number12
Early online date20 Oct 2016
Publication statusPublished - 21 Dec 2016


  • Salmonella enterica
  • anaerobic respiration
  • selenate reductase
  • protein-protein 45 interactions
  • twin-arginine signal peptide
  • system-specific chaperone


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