Research groups

Research

The theme of the group concerns the underlying mechanisms of protein secretion and membrane protein insertion. The process we study is fundamental to biology, found in every cell in every organism. The main focus is on the process that occurs in E. coli, where a channel in the plasma membrane SecYEG cooperates with specific energy transducing factors to drive proteins either across or into the membrane. We employ a variety of biophysical and biochemical methods to investigate the structure, kinetics and the dynamics of the protein translocation reaction. Ongoing projects focus on the mechanism of the core reaction driven by the ATPase SecA through SecYEG. Newer initiatives concern membrane protein insertion by YidC and protein transport in the context of the ‘holo’-translocon.

Group

Vicki Gold, Alice Robson, Ryan Schulze, Sarah Whitehouse, Constanze Ochmann and Oliver Drayton.

Funding: BBSRC, The Wellcome Trust

Recent publications

Robson, A., Gold, V. A., Hodson, S., Clarke, A. R. & Collinson, I. (2009). Energy transduction in protein transport and the ATP hydrolytic cycle of SecA. Proc Natl Acad Sci U S A 106, 5111-6.

Robson, A., Carr, B., Sessions, R. B. & Collinson, I. (2009). Synthetic peptides identify a second periplasmic site for the plug of the SecYEG protein translocation complex. FEBS Lett 583, 207-12.

Kohler, R., Boehringer, D., Greber, B., Bingel-Erlenmeyer, R., Collinson, I., Schaffitzel, C. & Ban, N. (2009). YidC and Oxa1 form dimeric insertion pores on the translating ribosome. Mol Cell 34, 344-53.

Bieniossek, C., Nie, Y., Frey, D., Olieric, N., Schaffitzel, C., Collinson, I., Romier, C., Berger, P., Richmond, T. J., Steinmetz, M. O. & Berger, I. (2009). Automated unrestricted multigene recombineering for multiprotein complex production. Nat Methods.