f.sargent@dundee.ac.uk

+44 (0) 1382 386463, internal ext. 86463


Molecular Microbiology, College of Life Sciences, University of Dundee

 

2001

A genetic screen for suppressors of Escherichia coli Tat signal peptide mutations establishes a critical role for the second arginine within the twin-arginine motif.
Archives of Microbiology 177: 107-112
(G. Buchanan, F. Sargent, B.C. Berks and T. Palmer)

Membrane interactions and self-association of the TatA and TatB components of the
twin-arginine translocation pathway.
FEBS Letters 506: 143-148
(E.de Leeuw, I. Porcelli, F. Sargent, T. Palmer and B.C. Berks)

Purified components of the Escherichia coli Tat protein transport system form a
double-layered ring structure.
European Journal of Biochemistry 268: 3361-3367
(F. Sargent, U. Gohlke, E. de Leeuw, N.R. Stanley, T. Palmer, H.R.Saibil and B.C. Berks)

A marriage of bacteriology with cell biology results in twin-arginines.
Trends in Microbiology 9: 196-198
(F. Sargent)

Constitutive expression of the Escherichia coli tat genes indicates an important role for the twin-arginine translocase during aerobic and anaerobic growth.
Journal of Bacteriology 183: 1801-1804
(R.L. Jack, F. Sargent, B.C. Berks, G. Sawers and T. Palmer)

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