Skip to main content Skip to navigation


1. van der Ploeg R., Barnett, J.P., Vasisht, N., Goosens, V. J., Poether, D. C., Robinson, C., and van Dijl, J. M. (2011) Salt-sensitivity of minimal Twin-arginine translocases. J Biol Chem. In Press

2. Barnett, J. P., Robinson C., Scanlan D. J., and Blindauer C (2011) The Tat protein export pathway and its role in cyanobacterial metalloprotein biosynthesis. FEMS Microbiol Lett. 325, 1-9.

3. Barnett, J. P., Lawrence, J., Mendel, S., and Robinson C (2011). Expression of the bifunctional Bacillus subtilis TatAd protein in Escherichia coli reveals distinct TatA/B-family and TatB specific domains. Arch Microbiol 193, 583-94.

4. Barnett, J. P., van der Ploeg R., Eijlander R. T., Nenninger A., Mendel S., Rozeboom R., Kuipers O. P., van Dijl JM., and Robinson C (2009). The twin-arginine translocation (Tat) systems from Bacillus subtilis display a conserved mode of complex organization and similar substrate recognition requirements. FEBS J 276, 232-43.

5. Mendel S., McCarthy A., Barnett, J. P., Eijlander R. T, Nenninger A, Kuipers O. P., and Robinson C (2008). The Escherichia coli TatABC system and a Bacillus subtilis TatAC-type system recognise three distinct targeting determinants in twin-arginine signal peptides. J Mol Biol 375, 661-72.

6. Barnett, J. P., Eijlander R. T., Kuipers O. P., and Robinson C (2008). A minimal Tat system from a gram-positive organism: a bifunctional TatA subunit participates in discrete TatAC and TatA complexes. J Biol Chem 283, 2534-42.

7. Oates J., Barrett C. M., Barnett, J. P., Byrne K. G., Bolhuis A., and Robinson C (2005). The Escherichia coli twin-arginine translocation apparatus incorporates a distinct form of TatABC complex, spectrum of modular TatA complexes and minor TatAB complex. J Mol Biol 346, 295-305.