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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{Yu:2018:10.1073/pnas.1800609115,
author = {Yu, J and Knoppova, J and Michoux, F and Bialek, W and Cota, Segura E and Shukla, M and Straskova, A and Aznar, G and Sobotka, R and Komenda, J and Murray, J and Nixon, PJ},
doi = {10.1073/pnas.1800609115},
journal = {Proceedings of the National Academy of Sciences},
pages = {E7824--E7833},
title = {Ycf48 involved in the biogenesis of the oxygen-evolving photosystem II complex is a seven-bladed beta-propeller protein},
url = {http://dx.doi.org/10.1073/pnas.1800609115},
volume = {115},
year = {2018}
}

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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Robust photosynthesis in chloroplasts and cyanobacteria requires the participation of accessory proteins to facilitate the assembly and maintenance of the photosynthetic apparatus located within the thylakoid membranes. The highly conserved Ycf48 protein acts early in the biogenesis of the oxygen-evolving photosystem II (PSII) complex by binding to newly synthesized precursor D1 subunit and by promoting efficient association with the D2 protein to form a PSII reaction center (PSII RC) assembly intermediate. Ycf48 is also required for efficient replacement of damaged D1 during the repair of PSII. However, the structural features underpinning Ycf48 function remain unclear. Here we show that Ycf48 proteins encoded by the thermophilic cyanobacterium Thermosynechococcus elongatus and the red alga Cyanidioschyzon merolae form seven-bladed beta-propellers with the 19-aa insertion characteristic of eukaryotic Ycf48 located at the junction of blades 3 and 4. Knowledge of these structures has allowed us to identify a conserved “Arg patch” on the surface of Ycf48 that is important for binding of Ycf48 to PSII RCs but also to larger complexes, including trimeric photosystem I (PSI). Reduced accumulation of chlorophyll in the absence of Ycf48 and the association of Ycf48 with PSI provide evidence of a more wide-ranging role for Ycf48 in the biogenesis of the photosynthetic apparatus than previously thought. Copurification of Ycf48 with the cyanobacterial YidC protein insertase supports the involvement of Ycf48 during the cotranslational insertion of chlorophyll-binding apopolypeptides into the membrane.
AU  - Yu,J
AU  - Knoppova,J
AU  - Michoux,F
AU  - Bialek,W
AU  - Cota,Segura E
AU  - Shukla,M
AU  - Straskova,A
AU  - Aznar,G
AU  - Sobotka,R
AU  - Komenda,J
AU  - Murray,J
AU  - Nixon,PJ
DO  - 10.1073/pnas.1800609115
EP  - 7833
PY  - 2018///
SN  - 0027-8424
SP  - 7824
TI  - Ycf48 involved in the biogenesis of the oxygen-evolving photosystem II complex is a seven-bladed beta-propeller protein
T2  - Proceedings of the National Academy of Sciences
UR  - http://dx.doi.org/10.1073/pnas.1800609115
UR  - http://hdl.handle.net/10044/1/61495
VL  - 115
ER  -