Structure of the TatC core of the twin-arginine protein transport system

Sarah E. Rollauer, Michael J. Tarry, James E. Graham, Mari Jääskeläinen, Franziska Jäger, Steven Johnson, Martin Krehenbrink, Sai-Man Liu, Michael J. Lukey, Julien Marcoux, Melanie A. McDowell, Fernanda Rodriguez, Pietro Roversi, Phillip J. Stansfeld, Carol V. Robinson, Mark S. P. Sansom, Tracy Palmer, Martin Högbom, Ben C. Berks () and Susan M. Lea ()
Additional contact information
Sarah E. Rollauer: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK
Michael J. Tarry: Stockholm Center for Biomembrane Research, Stockholm University, S-106 91 Stockholm, Sweden
James E. Graham: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK
Mari Jääskeläinen: Stockholm Center for Biomembrane Research, Stockholm University, S-106 91 Stockholm, Sweden
Franziska Jäger: College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK
Steven Johnson: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK
Martin Krehenbrink: University of Oxford, South Parks Road, Oxford OX1 3QU, UK
Sai-Man Liu: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK
Michael J. Lukey: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK
Julien Marcoux: Physical & Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK
Melanie A. McDowell: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK
Fernanda Rodriguez: University of Oxford, South Parks Road, Oxford OX1 3QU, UK
Pietro Roversi: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK
Phillip J. Stansfeld: University of Oxford, South Parks Road, Oxford OX1 3QU, UK
Carol V. Robinson: Physical & Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK
Mark S. P. Sansom: University of Oxford, South Parks Road, Oxford OX1 3QU, UK
Tracy Palmer: College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK
Martin Högbom: Stockholm Center for Biomembrane Research, Stockholm University, S-106 91 Stockholm, Sweden
Ben C. Berks: University of Oxford, South Parks Road, Oxford OX1 3QU, UK
Susan M. Lea: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK

Nature, 2012, vol. 492, issue 7428, 210-214

Abstract: Abstract The twin-arginine translocation (Tat) pathway is one of two general protein transport systems found in the prokaryotic cytoplasmic membrane and is conserved in the thylakoid membrane of plant chloroplasts. The defining, and highly unusual, property of the Tat pathway is that it transports folded proteins, a task that must be achieved without allowing appreciable ion leakage across the membrane. The integral membrane TatC protein is the central component of the Tat pathway. TatC captures substrate proteins by binding their signal peptides. TatC then recruits TatA family proteins to form the active translocation complex. Here we report the crystal structure of TatC from the hyperthermophilic bacterium Aquifex aeolicus. This structure provides a molecular description of the core of the Tat translocation system and a framework for understanding the unique Tat transport mechanism.

Date: 2012
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DOI: 10.1038/nature11683

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