Imperial College London
Alternate

Professor Dale Wigley FRS

Faculty of Medicine, Department of Infectious Disease

Chair in Protein Crystallography
 
 
 
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Contact

 

+44 (0)20 7594 8417d.wigley

 
 
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Assistant

 

Miss Kelly Butler +44 (0)20 7594 2763

 
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Location

 

258Sir Alexander Fleming BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Lin:2017:nar/gkx414,
author = {Lin, C-L and Chaban, Y and Rees, DM and McCormack, EA and Ocloo, L and Wigley, DB},
doi = {nar/gkx414},
journal = {Nucleic Acids Research},
pages = {7249--7260},
title = {Functional characterization and architecture of recombinant yeast SWR1 histone exchange complex},
url = {http://dx.doi.org/10.1093/nar/gkx414},
volume = {45},
year = {2017}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - We have prepared recombinant fourteen subunit yeast SWR1 complex from insect cells using a modified MultiBac system. The 1.07 MDa recombinant protein complex has histone-exchange activity. Full exchange activity is realized with a single SWR1 complex bound to a nucleosome. We also prepared mutant complexes that lack a variety of subunits or combinations of subunits and these start to reveal roles for some of these subunits as well as indicating interactions between them in the full complex. Complexes containing a series of N-terminally and C-terminally truncated Swr1 subunits reveal further details about interactions between subunits as well as their binding sites on the Swr1 subunit. Finally, we present electron microscopy studies revealing the dynamic nature of the complex and a 21 Å resolution reconstruction of the intact complex provides details not apparent in previously reported structures, including a large central cavity of sufficient size to accommodate a nucleosome.
AU  - Lin,C-L
AU  - Chaban,Y
AU  - Rees,DM
AU  - McCormack,EA
AU  - Ocloo,L
AU  - Wigley,DB
DO  - nar/gkx414
EP  - 7260
PY  - 2017///
SN  - 1362-4962
SP  - 7249
TI  - Functional characterization and architecture of recombinant yeast SWR1 histone exchange complex
T2  - Nucleic Acids Research
UR  - http://dx.doi.org/10.1093/nar/gkx414
UR  - http://hdl.handle.net/10044/1/48379
VL  - 45
ER  -
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