PDRA in Carbon Dioxide Signalling and Sustainability

The Role

Carbon dioxide and sustainability

Carbon dioxide is essential for life. It is at the beginning of every life process as a substrate for photosynthesis or chemosynthesis. It is at the end of every life process as the product of aerobic respiration and post-mortem decay. As such, it is not a surprise that this gas regulates such diverse processes as cellular chemical reactions, transport, maintenance of the cellular environment, behaviour and immunity. Carbon dioxide is a strategically important research target for crop responses to environmental change, insect-borne disease and public health. However, we know very little of the direct interactions of carbon dioxide with the cell, despite the importance of the gas to biology.

Carbon dioxide mediates the earliest known example of a protein post-translational modification (PTM), identified on haemoglobin in 1928. Carbon dioxide can directly combine with select protein groups to form carbamates. Influential research programmes from the 1920s-80s demonstrated that the carbamate PTM regulates oxygen-binding in haemoglobin and activates the carbon dioxide-fixing enzyme Rubisco. George Lorimer proposed carbamate PTMs to regulate biological responses to carbon dioxide in 1983. However, the carbamate PTM is unstable outside the cell, and its identification presents significant analytical challenges. Several stable carbamates have been identified in protein molecular structures. Still, the technical difficultie s in their widespread identification have resulted in carbon dioxide-mediated carbamylation being significantly understudied as a PTM.

Direct protein targets for carbon dioxide sensing are mainly unknown. We have developed technology to identify carbon dioxide-binding proteins systematically. We propose investigating a newly identified carbon dioxide binding site on Rubisco, the plant carbon dioxide-fixing enzyme. The project aims to understand how carbon dioxide regulates Rubisco function at a binding site distinct from the enzyme's active site and how this binding can be engineered to improve Rubisco's catalytic activity. The research programme will provide insight into direct molecular responses to carbon dioxide in prokaryotic and eukaryotic photosynthetic organisms. A significant outcome of this proposal will be photosynthetic organisms with enhanced yield in industrial and agricultural biotechnology. The work will be performed in collaboration with colleagues at Lancaster University.

The position offers an exciting opportunity to develop interdisciplinary biosciences and physical sciences skills. Please see here (pubmed.ncbi.nlm.nih.gov/?term=cann+mj&sort=pubdate&size=200) for publications from the PI in this and related fields.

The post is fixed term for 36 months, and the successful candidate will be working with Prof Martin Cann (PI; Dept of Biosciences) at Durham University.

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