title: A regulatory domain controls the transport activity of a twin-arginine signal peptide.
abstract: The twin-arginine translocation (Tat) pathway is used by bacteria for the transmembrane transport of folded proteins. Proteins are targeted to the Tat translocase by signal peptides that have common tripartite structures consisting of polar n-regions, hydrophobic h-regions, and polar c-regions. In this work, the signal peptide of [NiFe] hydrogenase-1 from Escherichia coli has been studied. The hydrogenase-1 signal peptide contains an extended n-region that has a conserved primary structure. Genetic and biochemical approaches reveal that the signal peptide n-region is essential for hydrogenase assembly and acts as a regulatory domain controlling transport activity of the signal peptide.
authors.affiliation: College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK.
authors.forename: Lisa
authors.initials: L
authors.lastname: Bowman
authors.forename: Tracy
authors.initials: T
authors.lastname: Palmer
authors.forename: Frank
authors.initials: F
authors.lastname: Sargent
mesh_terms: D000595:Amino Acid Sequence; D006864:Hydrogenase / Q000737:chemistry* / Q000235:genetics; D016296:Mutagenesis; D016297:Mutagenesis, Site-Directed; D021382:Protein Sorting Signals / Q000235:genetics*; D020133:Reverse Transcriptase Polymerase Chain Reaction
chemical_list: D021382:Protein Sorting Signals; D006864:Hydrogenase
keywords: Escherichia coli; Mutagenesis; Protein targeting; Signal peptide; Twin-arginine translocation pathway; [NiFe] hydrogenase