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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{Bebeacua:2012:10.1073/pnas.1114341109,
author = {Bebeacua, C and Förster, A and McKeown, C and Meyer, HH and Zhang, X and Freemont, PS},
doi = {10.1073/pnas.1114341109},
journal = {Proc Natl Acad Sci U S A},
pages = {1098--1103},
title = {Distinct conformations of the protein complex p97-Ufd1-Npl4 revealed by electron cryomicroscopy.},
url = {http://dx.doi.org/10.1073/pnas.1114341109},
volume = {109},
year = {2012}
}

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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - p97 is a key regulator of numerous cellular pathways and associates with ubiquitin-binding adaptors to remodel ubiquitin-modified substrate proteins. How adaptor binding to p97 is coordinated and how adaptors contribute to substrate remodeling is unclear. Here we present the 3D electron cryomicroscopy reconstructions of the major Ufd1-Npl4 adaptor in complex with p97. Our reconstructions show that p97-Ufd1-Npl4 is highly dynamic and that Ufd1-Npl4 assumes distinct positions relative to the p97 ring upon addition of nucleotide. Our results suggest a model for substrate remodeling by p97 and also explains how p97-Ufd1-Npl4 could form other complexes in a hierarchical model of p97-cofactor assembly.
AU  - Bebeacua,C
AU  - Förster,A
AU  - McKeown,C
AU  - Meyer,HH
AU  - Zhang,X
AU  - Freemont,PS
DO  - 10.1073/pnas.1114341109
EP  - 1103
PY  - 2012///
SP  - 1098
TI  - Distinct conformations of the protein complex p97-Ufd1-Npl4 revealed by electron cryomicroscopy.
T2  - Proc Natl Acad Sci U S A
UR  - http://dx.doi.org/10.1073/pnas.1114341109
VL  - 109
ER  -