Research

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Synthetic Biology underpins advances in the bioeconomy

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{Planamente:2016:10.15252/embj.201694024,
author = {Planamente, S and Salih, O and Manoli, E and Albesa-Jove, D and Freemont, PS and Filloux, AAM},
doi = {10.15252/embj.201694024},
journal = {EMBO Journal},
pages = {1613--1627},
title = {TssA forms a gp6-like ring attached to the type VI secretion sheath},
url = {http://dx.doi.org/10.15252/embj.201694024},
volume = {35},
year = {2016}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - The type VI secretion system (T6SS) is a supra-molecular bacterial complex that resembles phage tails. It is a killing machine which fires toxins into target cells upon contraction of its TssBC sheath. Here, we show that TssA1 is a T6SS component forming dodecameric ring structures whose dimensions match those of the TssBC sheath and which can accommodate the inner Hcp tube. The TssA1 ring complex binds the T6SS sheath and impacts its behaviour in vivo. In the phage, the first disc of the gp18 sheath sits on a baseplate wherein gp6 is a dodecameric ring. We found remarkable sequence and structural similarities between TssA1 and gp6 C-termini, and propose that TssA1 could be a baseplate component of the T6SS. Furthermore, we identified similarities between TssK1 and gp8, the former interacting with TssA1 while the latter is found in the outer radius of the gp6 ring. These observations, combined with similarities between TssF and gp6N-terminus or TssG and gp53, lead us to propose a comparative model between the phage baseplate and the T6SS.
AU  - Planamente,S
AU  - Salih,O
AU  - Manoli,E
AU  - Albesa-Jove,D
AU  - Freemont,PS
AU  - Filloux,AAM
DO  - 10.15252/embj.201694024
EP  - 1627
PY  - 2016///
SN  - 0261-4189
SP  - 1613
TI  - TssA forms a gp6-like ring attached to the type VI secretion sheath
T2  - EMBO Journal
UR  - http://dx.doi.org/10.15252/embj.201694024
UR  - http://hdl.handle.net/10044/1/33113
VL  - 35
ER  -
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