Tracy Palmer

Professor Tracy Palmer

Position: Professor of Molecular Microbiology and Head of the Division of Molecular Microbiology
Division: Molecular Microbiology
Address: College of Life Sciences, University of Dundee, Dundee
Telephone: +44 1382 386464, int ext. 86464
Email: t.palmer@dundee.ac.uk
Website: Palmer Lab

Protein transport across bacterial membranes

Research

Protein Transport in Bacteria

Figure 1. Transmission electron micrograph images of (left panel) E. coli K12 pa The major research focus of my group is the transport of proteins by the twin arginine protein transport pathway. This pathway, which is found in the cytoplasmic membranes of most bacteria, and the thylakoid membranes of plant chloroplasts, is highly unusual because it transports pre-folded proteins. Protein substrates are targeted to the Tat machinery by N-terminal signal peptides that contain an S/T- R-R-x-F-L-K ‘twin arginine’ motif. Our aims are to study the function and mechanism of the Tat protein transporter, and the contribution that it makes to the physiology of bacteria.

Functional studies on the bacterial Tat pathway are carried out in collaboration with Dr Ben Berks, University of Oxford. Using the model organism Escherichia coli, we have identified the tatA, tatB, tatC and tatE genes that encode components of the Tat system. Focusing on the major components, TatA, B and C we are studying their roles in protein transport by a combination of genetics, molecular biology and biochemical techniques.

 

Figure 2. Confocal fluoresence image of cells of <em> E.coli</em> K12 exporting Our physiological studies on the Tat pathway currently encompass two groups of bacteria. Escherichia coli K12 has some 27 or so Tat substrate proteins. About two thirds of these contain non-covalently bound redox cofactors that are bound prior to export by the Tat pathway. We collaborate with Professor Frank Sargent to genetically define the components required for the assembly of these complex Tat substrates before their interaction with the Tat system. Other substrates of the E. coli Tat system include two amidase enzymes involved in cell wall remodelling and that are critical for cell envelope integrity. In collaboration with the Drug Discovery Unit in the College of Life Sciences  we are interested in identifying small molecules that interfere with the activity of the Tat machinery that might be useful precursors to novel antimicrobial drugs

We have recently started collaborating with Prof Bill Hunter (Division of Biological Chemistry and Drug Discovery) to investigate the structure and function of Type VII protein secretion systems from Gram positive bacteria.

 


 

 

Teaching


Publications

  1. Fritsch, M.J., Krehenbrink, M., Tarry, M.J., Berks, B.C. and Palmer, T. (2012) “Processing by rhomboid protease is required for Providentia stuartii TatA to interact with TatC and to form functional homo-oligomeric complexes.” Molecular Microbiology in the press.
  2. Koch, S*., Fritsch, M.J*., Buchanan, G and Palmer, T. (2012) “The Escherichia coli TatA and TatB proteins have an N-out C-in topology in intact cells.” Journal of Biological Chemistry 287, 14420-14431.
  3.  Widdick, D., Matthew G. Hicks, M. G., Thompson, B. J., Tschumi, A., Chandra, G.,  Sutcliffe, I. C., Brülle, J. K., Sander, P., Palmer, T. and Hutchings, M. I. (2011) “Dissecting the complete lipoprotein biogenesis pathway in Streptomyces.”  Molecular Microbiology. 80, 1395-1412.
  4. Joshi, M.V., Mann, S.G., Antelmann, H., Widdick, D. Fyans, J.K., Chandra, G., Hutchings, M.I., Toth, I., Hecker, M., Loria, R. and Palmer, T. (2010) The Tat pathway exports multiple virulence proteins in the plant pathogen Streptomyces scabies Molecular Microbiology 77, 252-271.
  5. Handford, J.I. , Ize, B., Buchanan, G., Butland, G.P., Greenblatt, J., Emili, A. and Palmer, T. (2009) Conserved Network of Proteins Essential for Bacterial Viability. Journal of Bacteriology 191, 4732-4749
  6. Tarry, M.J., Schafer, E., Chen, S., Buchanan, G., Greene, N.P., Lea, S.M., Palmer, T., Saibil, H.R. and Berks, B.C. (2009) Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system. Proceedings of the National Academy of Sciences USA. 106, 13284-13289