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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{Aw:2021:10.1111/tra.12773,
author = {Aw, R and De, Wachter C and Laukens, B and De, Rycke R and De, Bruyne M and Bell, D and Callewaert, N and Polizzi, KM},
doi = {10.1111/tra.12773},
journal = {Traffic},
pages = {48--63},
title = {Knockout of RSN1, TVP18 or CSC12 causes perturbation of Golgi cisternae in Pichia pastoris},
url = {http://dx.doi.org/10.1111/tra.12773},
volume = {22},
year = {2021}
}

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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - The structural organization of the Golgi stacks in mammalian cells is intrinsically linked to function, including glycosylation, but the role of morphology is less clear in lower eukaryotes. Here we investigated the link between the structural organization of the Golgi and secretory pathway function using Pichia pastoris as a model system. To unstack the Golgi cisternae, we disrupted 18 genes encoding proteins in the secretory pathway without loss of viability. Using biosensors, confocal microscopy and transmission electron microscopy we identified three strains with irreversible perturbations in the stacking of the Golgi cisternae, all of which had disruption in genes that encode proteins with annotated function as or homology to calcium/calcium permeable ion channels. Despite this, no variation in the secretory pathway for ER size, whole cell glycomics or recombinant protein glycans was observed. Our investigations showed the robust nature of the secretory pathway in P. pastoris and suggest that Ca2+ concentration, homeostasis or signalling may play a significant role for Golgi stacking in this organism and should be investigated in other organisms.
AU  - Aw,R
AU  - De,Wachter C
AU  - Laukens,B
AU  - De,Rycke R
AU  - De,Bruyne M
AU  - Bell,D
AU  - Callewaert,N
AU  - Polizzi,KM
DO  - 10.1111/tra.12773
EP  - 63
PY  - 2021///
SN  - 1398-9219
SP  - 48
TI  - Knockout of RSN1, TVP18 or CSC12 causes perturbation of Golgi cisternae in Pichia pastoris
T2  - Traffic
UR  - http://dx.doi.org/10.1111/tra.12773
UR  - https://onlinelibrary.wiley.com/doi/10.1111/tra.12773
UR  - http://hdl.handle.net/10044/1/85103
VL  - 22
ER  -