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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{Schuster:2016:10.1126/scisignal.aaf7279,
author = {Schuster, C and Bellows, L and Tosi, T and Campeotto and Corrigan and Freemont, P and Grundling, A},
doi = {10.1126/scisignal.aaf7279},
journal = {Science Signaling},
pages = {ra81--ra81},
title = {The second messenger c-di-AMP inhibits the osmolyte uptake system OpuC in Staphylococcus aureus},
url = {http://dx.doi.org/10.1126/scisignal.aaf7279},
volume = {9},
year = {2016}
}

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RIS format (EndNote, RefMan)

TY - JOUR
AB - Staphylococcus aureus is an important opportunistic human pathogen that is highly resistant to osmotic stresses. To survive an increase in osmolarity, bacteria immediately take up potassium ions and small organic compounds known as compatible solutes. The second messenger cyclic diadenosine monophosphate (c-di-AMP) reduces the ability of bacteria to withstand osmotic stress by binding to and inhibiting several proteins that promote potassium uptake. We identified OpuCA, the adenosine triphosphatase (ATPase) component of an uptake system for the compatible solute carnitine, as a c-di-AMP target protein in S. aureus and found that the LACΔgdpP strain of S. aureus, which overproduces c-di-AMP, showed reduced carnitine uptake. The paired cystathionine-β-synthase (CBS) domains of OpuCA bound to c-di-AMP, and a crystal structure revealed a putative binding pocket for c-di-AMP in the cleft between the two CBS domains. Thus, c-di-AMP inhibits osmoprotection through multiple mechanisms.
AU - Schuster,C
AU - Bellows,L
AU - Tosi,T
AU - Campeotto
AU - Corrigan
AU - Freemont,P
AU - Grundling,A
DO - 10.1126/scisignal.aaf7279
EP - 81
PY - 2016///
SN - 1945-0877
SP - 81
TI - The second messenger c-di-AMP inhibits the osmolyte uptake system OpuC in Staphylococcus aureus
T2 - Science Signaling
UR - http://dx.doi.org/10.1126/scisignal.aaf7279
UR - http://stke.sciencemag.org/cgi/reprint/sigtrans;9/441/ra81?ijkey=SZluRyjzK/0hw&keytype=ref&siteid=sigtrans
UR - http://hdl.handle.net/10044/1/39084
VL - 9
ER -