1887

Abstract

serovar Typhimurium is a Gram-negative bacterium with a flexible respiratory capability. Under anaerobic conditions, can utilize a range of terminal electron acceptors, including selenate, to sustain respiratory electron transport. The selenate reductase is a membrane-bound enzyme encoded by the 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 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.

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2016-12-21
2020-08-04
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