Protein transport by the bacterial Tat pathway
Event details
| Date | 03.05.2016 |
| Hour | 12:15 |
| Speaker | Prof. Tracy Palmer, University of Dundee, Scotland |
| Location | |
| Category | Conferences - Seminars |
The Tat protein transport system functions to export folded proteins across the bacterial cytoplasmic membrane. Many Tat substrate proteins bind complex metal cofactors and the Tat pathway is required for important bacterial cellular processes including respiration and photosynthesis, cell division, motility and iron and phosphate acquisition. The Tat system is found in many animal and plant bacterial pathogens where in most cases it is required for virulence.
Proteins are targeted to the Tat system by N-terminal signal peptides that contain a conserved twin arginine motif. Our studies with the model organism Escherichia coli have shown that the integral membranes proteins TatA, TatB, and TatC form essential components of the transport machinery. Multiple copies of TatB and TatC associate to form a large TatBC complex that recognises twin-arginine signal peptides and binds substrate proteins. Binding of substrate proteins to TatBC triggers polymerization of TatA to form the transmembrane translocation pathway.
Recently the crystal structure of the TatC component from Aquifex aeolicus has been determined. TatC contains six closely-packed transmembrane helices forming a central cavity on one face of the protein overhung by an extensive periplasmic cap [1]. This structure forms a framework for understanding the location and dynamic nature of the binding sites for the TatA and TatB partner proteins and the twin-arginine signal peptide. We have been using a combination of molecular biology, suppression genetics and cross-linking studies to explore the molecular interactions between the Tat components at different stages of the Tat translocation cycle. Our latest findings will be presented.
1. Rollauer, S.E., et al. Nature 2012, 492, 210-214.
Bio: Since 2007 - Professor of Molecular Microbiology, Head of the Division of Molecular Microbiology, College of Life Sciences, University of Dundee
2004-2007 - MRC Senior Non Clinical Research Fellow based at John Innes Centre, Norwich
1996-2004 - Royal Society University Research Fellow based at John Innes Centre, Norwich
1993-1996 - University Research Fellow, Department of Biochemistry, University of Dundee
1992-1993 - Postdoctoral Research Assistant, University of Dundee with Prof D.H. Boxer
1988-1991 - Research Associate (RA1B) and PhD student, University of Birmingham with Prof J.B. Jackson
1988-1991 - Postgraduate:Ph.D. Biochemistry, University of Birmingham
1985-1988 - Undergraduate:B. Sc. Biochemistry (First Class Honours),University of Birmingham
Proteins are targeted to the Tat system by N-terminal signal peptides that contain a conserved twin arginine motif. Our studies with the model organism Escherichia coli have shown that the integral membranes proteins TatA, TatB, and TatC form essential components of the transport machinery. Multiple copies of TatB and TatC associate to form a large TatBC complex that recognises twin-arginine signal peptides and binds substrate proteins. Binding of substrate proteins to TatBC triggers polymerization of TatA to form the transmembrane translocation pathway.
Recently the crystal structure of the TatC component from Aquifex aeolicus has been determined. TatC contains six closely-packed transmembrane helices forming a central cavity on one face of the protein overhung by an extensive periplasmic cap [1]. This structure forms a framework for understanding the location and dynamic nature of the binding sites for the TatA and TatB partner proteins and the twin-arginine signal peptide. We have been using a combination of molecular biology, suppression genetics and cross-linking studies to explore the molecular interactions between the Tat components at different stages of the Tat translocation cycle. Our latest findings will be presented.
1. Rollauer, S.E., et al. Nature 2012, 492, 210-214.
Bio: Since 2007 - Professor of Molecular Microbiology, Head of the Division of Molecular Microbiology, College of Life Sciences, University of Dundee
2004-2007 - MRC Senior Non Clinical Research Fellow based at John Innes Centre, Norwich
1996-2004 - Royal Society University Research Fellow based at John Innes Centre, Norwich
1993-1996 - University Research Fellow, Department of Biochemistry, University of Dundee
1992-1993 - Postdoctoral Research Assistant, University of Dundee with Prof D.H. Boxer
1988-1991 - Research Associate (RA1B) and PhD student, University of Birmingham with Prof J.B. Jackson
1988-1991 - Postgraduate:Ph.D. Biochemistry, University of Birmingham
1985-1988 - Undergraduate:B. Sc. Biochemistry (First Class Honours),University of Birmingham
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Organizer
- Stewart Cole