Skip to main content

The Twin-Arginine Pathway for Protein Secretion

Frain, Kelly M. and van Dijl, Jan Maarten and Robinson, Colin (2019) The Twin-Arginine Pathway for Protein Secretion. In: Sandkvist, Maria and Cascales, Eric and Christie, Peter J., eds. Protein Secretion in Bacteria. American Society for Microbiology. ISBN 978-1-68367-027-8. E-ISBN 978-1-68367-028-5. (doi:10.1128/ecosalplus.ESP-0040-2018) (KAR id:74552)

PDF Author's Accepted Manuscript
Language: English
Download (1MB) Preview
[thumbnail of Kelly review 2019 - EcoSal Plus.pdf]
This file may not be suitable for users of assistive technology.
Request an accessible format
Official URL:


About 20 to 30% of proteins synthesized in the bacterial cytoplasm are destined for extracytoplasmic locations ( 1 ). They pass the cytoplasmic membrane using specialized transport systems, involving gated pores, energy, and signal peptides to direct protein export. Two major protein export systems are known, namely, the general secretory (Sec) pathway and the twin-arginine translocation (Tat) pathway ( Fig. 1 ). Most proteins use the Sec pathway, common to all domains of life. The Tat pathway, the focus of this review, is more exclusive. For example, it has only ∼30 native substrates in the Gram-negative bacterium Escherichia coli, and it is not universally conserved ( 2 ).

Item Type: Book section
DOI/Identification number: 10.1128/ecosalplus.ESP-0040-2018
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Susan Davies
Date Deposited: 24 Jun 2019 14:43 UTC
Last Modified: 09 Dec 2022 00:52 UTC
Resource URI: (The current URI for this page, for reference purposes)
Robinson, Colin:
  • Depositors only (login required):


Downloads per month over past year