Invited seminar at the Institute for
Molecular Cell and Systems Biology
#MCSBSem
26.04.2016
Prof. Tracy Palmer
University of Dundee
More about Tracy's work: http://www.lifesci.dundee.ac.uk/people/tracy-palmer
Some of the papers mentioned in the talk:
Alcock, F, Baker, MAB, Greene, NP, Palmer, T, Wallace, MI and Ben C. Berks 2013 Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system. 110 E3650-9.
Cleon, F., Habersetzer, J., Alcock, F., Kneuper, H., Stansfeld, P. J., Basit, H., Wallace, M. I., Berks, B. C. and Palmer, T. (2015) The TatC component of the twin-arginine protein translocase functions as an obligate oligomer. Mol Microbiol. 98, 111-129
Gohlke, U et al. The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter. PNAS 2005 102 (30) 10482-10486
Palmer, T, BC Berks 2012 The twin-arginine translocation (Tat) protein export pathway. Nature Reviews Microbiology 10 (7), 483-496
Rollauer, et al. (2012) Structure of the TatC core of the twin-arginine protein transport system. Nature. 492, 210-214
Tarry, MJ et al. Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system. PNAS 106 (32), 13284-13289.
Thomas et al. 2001 Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli. Molecular Microbiology 39: 47-53.
Rollauer, et al. (2012) Structure of the TatC core of the twin-arginine protein transport system. Nature. 492, 210-214
Tarry, MJ et al. Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system. PNAS 106 (32), 13284-13289.
Thomas et al. 2001 Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli. Molecular Microbiology 39: 47-53.