A regulatory domain controls the transport activity of a twin-arginine signal peptide

Lisa Bowman; Tracy Palmer; Frank Sargent

doi:10.1016/j.febslet.2013.09.005

A regulatory domain controls the transport activity of a twin-arginine signal peptide

Lisa Bowman, Tracy Palmer, Frank Sargent (Lead / Corresponding author)

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

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.

Original language	English
Pages (from-to)	3365-3370
Number of pages	6
Journal	FEBS Letters
Volume	587
Issue number	20
DOIs	https://doi.org/10.1016/j.febslet.2013.09.005
Publication status	Published - 11 Oct 2013

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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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AB - 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.

U2 - 10.1016/j.febslet.2013.09.005

DO - 10.1016/j.febslet.2013.09.005

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JO - FEBS Letters

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A regulatory domain controls the transport activity of a twin-arginine signal peptide

Abstract

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