Professor Colin Robinson joined the School of Biosciences in 2013. He studied Biochemistry as an undergraduate at the University of Edinburgh and went on to carry out a PhD studying chloroplast protein targeting with John Ellis at the University of Warwick. This generated a long-standing interest in protein targeting systems which has remained a dominant interest in the research group. After completing his PhD he spent 2 years at the University of Munich studying mitochondrial protein targeting with Professor Walter Neupert. He then returned to Warwick as a lecturer in 1985 and spent the next 27 years at Warwick as Lecturer, Senior lecturer and finally Professor. Much of the research in the Robinson lab is focused on the mechanisms by which proteins are transported into and across biological membranes, with a particular focus on the bacterial protein export system, Tat. Current research in the lab involves the exploitation of bacterial protein export systems for the production of high value recombinant proteins, as well as investigation of the unique proofreading mechanism of the bacterial and plant Tat systems.
Colin is a member of the Industrial Biotechnology and Synthetic Biology Group and the Industrial Biotechnology Centre
Understanding and exploiting (i) protein transport systems in bacteria and chloroplasts, and (ii) pathways for high-value products in microalgae
Protein transport systems
Much our research is focused on the mechanisms by which proteins are transported into and across biological membranes. In particular, we are interested in bacterial protein export. Bacteria export numerous proteins into the periplasm (Gram-negative species) or the cell wall/medium (Gram-positives) and the underlying mechanisms have been studied in great detail. Many proteins are exported using the Sec-dependent pathway, in which substrates are 'threaded' through the membrane-bound Sec translocon in an unfolded state. Other proteins are exported by the twin-arginine translocation, or Tat pathway. In this pathway, substrates are synthesised with N-terminal signal peptides containing a key twin-arginine motif. The proteins are then transported by a membrane-bound Tat translocon which is uniquely able to transport fully folded proteins - even oligomeric proteins - across the tightly coupled plasma membrane. Ongoing projects are aimed at understanding how this is achieved, and how the system can be expolited for the production of high-value therapeutic proteins.
Microalgae (which we define here as cyanobacteria and unicellular eukaryotic algae) hold great promise for the biotechnology industry. They divide rapidly, can be grown under phototrophic conditions, and contain a variety of high-value compounds including colourants and oils. However, they also have real potential as cell factories. As part of a large EU-funded consortium, we are developing strains that express pathways for high-value compounds, using the cyanobacterium Synechocystis PCC6803 and the alga Chlamydomonas reinhardtii as host organisms. We are also expressing high-value biotherapeutics in Chlamydomonas in order to assess this organism's potential as a protein production host.
GCRF Establishment of biopharmaceutical and animal vaccine production capacity in Thailand and SE Asia
IB Catalyst project to develop a suite of new tools for production of recombinant proteins in E. coli
The bacterial and plant Tat systems - unique mechanism and remarkable 'proofreading' abilites
Marie Sklodowska-Curie project, 'ProteinFactory'