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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{Yeung:2014:10.1098/rsob.130142,
author = {Yeung, HO and Foerster, A and Bebeacua, C and Niwa, H and Ewens, C and McKeown, C and Zhang, X and Freemont, PS},
doi = {10.1098/rsob.130142},
journal = {Open Biology},
title = {Inter-ring rotations of AAA ATPase p97 revealed by electron cryomicroscopy},
url = {http://dx.doi.org/10.1098/rsob.130142},
volume = {4},
year = {2014}
}

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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - The type II AAA+ protein p97 is involved in numerous cellular activities, including endoplasmic reticulum-associated degradation, transcription activation, membrane fusion and cell-cycle control. These activities are at least in part regulated by the ubiquitin system, in which p97 is thought to target ubiquitylated protein substrates within macromolecular complexes and assist in their extraction or disassembly. Although ATPase activity is essential for p97 function, little is known about how ATP binding or hydrolysis is coupled with p97 conformational changes and substrate remodelling. Here, we have used single-particle electron cryomicroscopy (cryo-EM) to study the effect of nucleotides on p97 conformation. We have identified conformational heterogeneity within the cryo-EM datasets from which we have resolved two major p97 conformations. A comparison of conformations reveals inter-ring rotations upon nucleotide binding and hydrolysis that may be linked to the remodelling of target protein complexes.
AU  - Yeung,HO
AU  - Foerster,A
AU  - Bebeacua,C
AU  - Niwa,H
AU  - Ewens,C
AU  - McKeown,C
AU  - Zhang,X
AU  - Freemont,PS
DO  - 10.1098/rsob.130142
PY  - 2014///
SN  - 2046-2441
TI  - Inter-ring rotations of AAA ATPase p97 revealed by electron cryomicroscopy
T2  - Open Biology
UR  - http://dx.doi.org/10.1098/rsob.130142
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000333906500001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - http://hdl.handle.net/10044/1/69629
VL  - 4
ER  -