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Research

Biological systems - including the simplest cells - exhibit a broad range of functions to thrive in their environment. Research in the Imperial College Centre for Synthetic Biology is focused on the possibility of engineering the underlying biochemical processes to solve many of the challenges facing society, from healthcare to sustainable energy. In particular, we model, analyse, design and build biological and biochemical systems in living cells and/or in cell extracts, both exploring and enhancing the engineering potential of biology.

As part of our research we develop novel methods to accelerate the celebrated Design-Build-Test-Learn synthetic biology cycle. As such research in the Centre for Synthetic Biology highly multi- and interdisciplinary covering computational modelling and machine learning approaches; automated platform development and genetic circuit engineering ; multi-cellular and multi-organismal interactions, including gene drive and genome engineering; metabolic engineering; in vitro/cell-free synthetic biology; engineered phages and directed evolution; and biomimetics, biomaterials and biological engineering.

Publications

Citation

BibTex format

@article{McFarlane:2018:10.1101/414334,
author = {McFarlane, C and Shah, N and Kabasakal, B and Cotton, CAR and Bubeck, D and Murray, J},
doi = {10.1101/414334},
journal = {biorxiv},
title = {Structural basis of light-induced redox regulation in the Calvin cycle},
url = {http://dx.doi.org/10.1101/414334},
year = {2018}
}

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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Abstract In plants, carbon dioxide is fixed via the Calvin cycle in a tightly regulated process. Key to this regulation is the conditionally disordered protein CP12. CP12 forms a complex with two Calvin cycle enzymes, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase (PRK), inhibiting their activities. The mode of CP12 action was unknown. By solving crystal structures of CP12 bound to GAPDH, and the ternary GAPDH-CP12-PRK complex by electron cryo-microscopy, we reveal that formation of the N-terminal disulfide pre-orders CP12 prior to binding the PRK active site. We find that CP12 binding to GAPDH influences substrate accessibility of all GAPDH active sites in the binary and ternary inhibited complexes. Our model explains how CP12 integrates responses from both redox state and nicotinamide dinucleotide availability to regulate carbon fixation. One Sentence Summary How plants turn off carbon fixation in the dark.
AU  - McFarlane,C
AU  - Shah,N
AU  - Kabasakal,B
AU  - Cotton,CAR
AU  - Bubeck,D
AU  - Murray,J
DO  - 10.1101/414334
PY  - 2018///
TI  - Structural basis of light-induced redox regulation in the Calvin cycle
T2  - biorxiv
UR  - http://dx.doi.org/10.1101/414334
ER  -

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