A regulatory domain controls the transport activity of a twin-arginine signal peptide |
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Authors: | Lisa Bowman Tracy PalmerFrank Sargent |
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Affiliation: | College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK |
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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. |
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Keywords: | Protein targeting Twin-arginine translocation pathway [NiFe] hydrogenase Signal peptide Mutagenesis Escherichia coli |
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