We are interested in both fundamental studies of membrane proteins and in how this particular class of proteins might be used in synthetic biology. Current projects are:

Biomineralization. Inorganic minerals are widespread and diverse in nature, being important constituents of structures including bone, tooth and shell. However, the underlying biological mechanisms behind biomineral synthesis remain only partly understood. We are interested in the roles played by membrane transport proteins in biomineralization. Our initial target is a unique family of membrane proteins found in the diatoms, unicellular algae that sheath themselves in an intricate outer cell wall made of silica. To build this ‘glass house’, diatoms have evolved a novel family of integral membrane proteins that can transport a silica precursor across the cell membrane envelope. We are conducting the first biochemical and biophysical studies of these silicon transporters to try and understand their structure and function at the molecular level. By reconstituting these transporters into synthetic lipid vesicles, we aim to construct a simple model of a diatom cell. We intend to extend this approach in order to better understand the synthesis of other important biominerals such as calcium carbonate, calcium phosphate and iron oxide.

Aromatic acid transport. Aromatic acids are transported into certain bacterial cells via a dedicated family of membrane transport proteins. We have recently begun to study the structure and function of these proteins to understand how members of this family recognize and transport aromatic acids. We are also currently exploring whether we can apply these proteins as components of cellular computers, by using them to form biochemical logic gates.

Yeast acyltransferases. Brewer’s yeast contains a number of membrane-associated enzymes (acyltransferases) that make biochemicals which control the flavour of fermented beverages such as wine and beer. We have developed novel methods to understand the structure and function of these enzymes and are now curious as to whether they could be used as environmentally-friendly ‘cell factories’ for the production of fragrances and fine chemicals.