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Twin-Arginine Protein Translocation

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Protein and Sugar Export and Assembly in Gram-positive Bacteria

Part of the book series: Current Topics in Microbiology and Immunology ((CT MICROBIOLOGY,volume 404))

Abstract

Twin-arginine protein translocation systems (Tat) translocate fully folded and co-factor-containing proteins across biological membranes. In this review, we focus on the Tat pathway of Gram-positive bacteria. The minimal Tat pathway is composed of two components, namely a TatA and TatC pair, which are often complemented with additional TatA-like proteins. We provide overviews of our current understanding of Tat pathway composition and mechanistic aspects related to Tat-dependent cargo protein translocation. This includes Tat pathway flexibility, requirements for the correct folding and incorporation of co-factors in cargo proteins and the functions of known cargo proteins. Tat pathways of several Gram-positive bacteria are discussed in detail, with emphasis on the Tat pathway of Bacillus subtilis. We discuss both shared and unique features of the different Gram-positive bacterial Tat pathways. Lastly, we highlight topics for future research on Tat, including the development of this protein transport pathway for the biotechnological secretion of high-value proteins and its potential applicability as an antimicrobial drug target in pathogens.

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Abbreviations

Sec pathway:

General Secretory pathway

Tat:

Twin-arginine translocation

NMR:

Nuclear magnetic resonance

Y2H:

Yeast two-hybrid

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Acknowledgements

VJG and JMvD were in parts supported by the CEU projects PITN-GA-2008-215524 (TranSys), LSHG-CT-2006-037469 and 244093, and the transnational SysMO initiative through projects BACELL SysMO1 and 2 with funding from the Research Council for Earth and Life Sciences of the Netherlands Organization for Scientific Research (NWO-ALW).

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  1. MRC Centre for Molecular Bacteriology and Infection, Section of Microbiology, Imperial College London, London, SW7 2AZ, UK

    Vivianne J. Goosens

  2. Department of Medical Microbiology, University of Groningen, University Medical Center Groningen, Hanzeplein 1, P.O. Box 30001, 9700, RB, Groningen, The Netherlands

    Jan Maarten van Dijl

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  1. Vivianne J. Goosens
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Correspondence to Jan Maarten van Dijl .

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  1. GSK Vaccines , Siena, Siena, Italy

    Fabio Bagnoli

  2. GSK Vaccines , Siena, Italy

    Rino Rappuoli

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Goosens, V.J., van Dijl, J.M. (2016). Twin-Arginine Protein Translocation. In: Bagnoli, F., Rappuoli, R. (eds) Protein and Sugar Export and Assembly in Gram-positive Bacteria . Current Topics in Microbiology and Immunology, vol 404. Springer, Cham. https://doi.org/10.1007/82_2016_7

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