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Molecular insights into type I secretion systems

  • Michael H.H. Lenders

    Michael Lenders studied Biochemistry at the Heinrich Heine University in Düsseldorf and graduated in 2012. His master thesis about the characterization of self-inserting membrane proteins by atomic force microscopy was prepared in cooperation with the Swiss Federal Institute of Technology Zürich. Since 2012, he is a PhD student focusing structural and functional characterization of the membrane fusion protein of the haemolysin A T1SS at the institute of Biochemistry, Heinrich Heine University Düsseldorf.

    , Sven Reimann

    Sven Reimann studied Biochemistry at the Heinrich Heine University Düsseldorf. He did his Master’s degree at the Forschungszentrum Jülich investigating a putative virulence factor of Pseudomonas aeruginosa. Since then he has been doing his PhD at the Institute of Biochemistry at a Heinrich Heine University Düsseldorf. His research field is the hemolysis A type 1 secretion system of Escherichia coli and particularly the ABC transporter HlyB.

    , Sander H. J. Smits

    Sander Smits obtained his PhD in Biochemistry at the Institute of Biochemistry, Heinrich Heine University Düsseldorf in 2008. Since then he has worked as a senior scientist with a special focus on membrane transporter, especially on the transporter of large unfolded proteins as well as peptides having an antimicrobial activity.

    and Lutz Schmitt

    Lutz Schmitt studied Chemistry at the University of Freiburg and obtained his PhD from the Technical University Munich. After a Post Doc at Stanford University, he moved as a DFG-funded Emmy Noether Fellow to the Universities of Marburg and Frankfurt. In 2005 he was appointed as Professor of Biochemistry at the Heinrich Heine University Düsseldorf where he became full professor in 2008. His research interest are recognition processes at membranes and transport across membranes with an emphasis on ABC transporters.

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Published/Copyright: July 5, 2013

Abstract

Type 1 secretion systems are one of the main machineries in Gram-negative bacteria involved in the secretion of a wide range of substrates from the cytoplasm across the inner and outer membrane in one step to the extracellular space. The range of substrates varies from small proteins up to large surface layer proteins of about 900 kDa. Most of the substrates have a non-cleavable C-terminal secretion signal and so-called GG repeats that are able to bind calcium ions. The translocator complex is composed of a trimeric outer membrane protein that provides a pore in the outer membrane. A multimeric membrane fusion protein spans the periplasm and forms a continuous channel connecting the outer membrane protein with a dimeric ATP-binding cassette transporter in the inner membrane. The ATP-binding cassette-transporter is thought to form a channel through the inner membrane and energizes the transport process. This review will provide a detailed view of the components of the translocator and will summarize structural as well as functional data.


Corresponding author: Lutz Schmitt, Institute of Biochemistry, Heinrich Heine University, Universitätsstraße 1, D-40225 Düsseldorf, Germany, e-mail:

About the authors

Michael H.H. Lenders

Michael Lenders studied Biochemistry at the Heinrich Heine University in Düsseldorf and graduated in 2012. His master thesis about the characterization of self-inserting membrane proteins by atomic force microscopy was prepared in cooperation with the Swiss Federal Institute of Technology Zürich. Since 2012, he is a PhD student focusing structural and functional characterization of the membrane fusion protein of the haemolysin A T1SS at the institute of Biochemistry, Heinrich Heine University Düsseldorf.

Sven Reimann

Sven Reimann studied Biochemistry at the Heinrich Heine University Düsseldorf. He did his Master’s degree at the Forschungszentrum Jülich investigating a putative virulence factor of Pseudomonas aeruginosa. Since then he has been doing his PhD at the Institute of Biochemistry at a Heinrich Heine University Düsseldorf. His research field is the hemolysis A type 1 secretion system of Escherichia coli and particularly the ABC transporter HlyB.

Sander H. J. Smits

Sander Smits obtained his PhD in Biochemistry at the Institute of Biochemistry, Heinrich Heine University Düsseldorf in 2008. Since then he has worked as a senior scientist with a special focus on membrane transporter, especially on the transporter of large unfolded proteins as well as peptides having an antimicrobial activity.

Lutz Schmitt

Lutz Schmitt studied Chemistry at the University of Freiburg and obtained his PhD from the Technical University Munich. After a Post Doc at Stanford University, he moved as a DFG-funded Emmy Noether Fellow to the Universities of Marburg and Frankfurt. In 2005 he was appointed as Professor of Biochemistry at the Heinrich Heine University Düsseldorf where he became full professor in 2008. His research interest are recognition processes at membranes and transport across membranes with an emphasis on ABC transporters.

We thank all members of the Institute of Biochemistry, Heinrich-Heine-Universität Düsseldorf, for helpful and very fruitful discussions. We gratefully acknowledge support (and training) from the International NRW Research School BioStruct, granted by the Ministry of Innovation, Science and Research of the State North Rhine-Westphalia, the Heinrich-Heine-University Düsseldorf, and the Entrepreneur Foundation at the Heinrich-Heine-University of Düsseldorf. Apologies to all our colleagues who contributed to our current understanding of T1SS but were not referenced due to space limitations.

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Received: 2013-5-6
Accepted: 2013-7-2
Published Online: 2013-07-05
Published in Print: 2013-11-01

©2013 by Walter de Gruyter Berlin Boston

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  3. Guest Editorial
  4. Highlight: NRW Research School BioStruct – Biological Structures in Molecular Medicine and Biotechnology
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