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

Author

Listed:
  • Sarah E. Rollauer

    (Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK
    University of Oxford, South Parks Road, Oxford OX1 3QU, UK)

  • Michael J. Tarry

    (Stockholm Center for Biomembrane Research, Stockholm University, S-106 91 Stockholm, Sweden
    Present addresses: Department of Biochemistry, McGill University Room 457, Bellini Life Science Complex, 3649 Promenade Sir William Osler, Montreal, Quebec H3G 0B1, Canada (M.J.T.); 306 Briggs Hall, Department of Microbiology, University of California Davis, One Shields Avenue, Davis, California 95616-2866, USA (J.E.G.); Department of Molecular Medicine, Cornell University, Ithaca, New York 14853, USA (M.J.L.); CIC bioGUNE, Parque Tecnologico de Bizkaia, 48160 Dorio, Bizkaia, Spain (P.R.).)

  • James E. Graham

    (Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK
    University of Oxford, South Parks Road, Oxford OX1 3QU, UK
    Present addresses: Department of Biochemistry, McGill University Room 457, Bellini Life Science Complex, 3649 Promenade Sir William Osler, Montreal, Quebec H3G 0B1, Canada (M.J.T.); 306 Briggs Hall, Department of Microbiology, University of California Davis, One Shields Avenue, Davis, California 95616-2866, USA (J.E.G.); Department of Molecular Medicine, Cornell University, Ithaca, New York 14853, USA (M.J.L.); CIC bioGUNE, Parque Tecnologico de Bizkaia, 48160 Dorio, Bizkaia, Spain (P.R.).)

  • 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
    University of Oxford, South Parks Road, Oxford OX1 3QU, UK)

  • Michael J. Lukey

    (Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK
    University of Oxford, South Parks Road, Oxford OX1 3QU, UK
    Present addresses: Department of Biochemistry, McGill University Room 457, Bellini Life Science Complex, 3649 Promenade Sir William Osler, Montreal, Quebec H3G 0B1, Canada (M.J.T.); 306 Briggs Hall, Department of Microbiology, University of California Davis, One Shields Avenue, Davis, California 95616-2866, USA (J.E.G.); Department of Molecular Medicine, Cornell University, Ithaca, New York 14853, USA (M.J.L.); CIC bioGUNE, Parque Tecnologico de Bizkaia, 48160 Dorio, Bizkaia, Spain (P.R.).)

  • 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
    Present addresses: Department of Biochemistry, McGill University Room 457, Bellini Life Science Complex, 3649 Promenade Sir William Osler, Montreal, Quebec H3G 0B1, Canada (M.J.T.); 306 Briggs Hall, Department of Microbiology, University of California Davis, One Shields Avenue, Davis, California 95616-2866, USA (J.E.G.); Department of Molecular Medicine, Cornell University, Ithaca, New York 14853, USA (M.J.L.); CIC bioGUNE, Parque Tecnologico de Bizkaia, 48160 Dorio, Bizkaia, Spain (P.R.).)

  • 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)

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.

Suggested Citation

  • 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. McDowe, 2012. "Structure of the TatC core of the twin-arginine protein transport system," Nature, Nature, vol. 492(7428), pages 210-214, December.
    • Handle: RePEc:nat:nature:v:492:y:2012:i:7428:d:10.1038_nature11683
    DOI: 10.1038/nature11683
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