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{Zhang:2017:10.1038/s41594-017-0003-7,
author = {Zhang, X and Aramayo, RJ and Willhoft, O and Ayala, R and Bythell-Douglas, R and Wigley, DB},
doi = {10.1038/s41594-017-0003-7},
journal = {Nature Structural and Molecular Biology},
pages = {37--44},
title = {CryoEM structures of the human INO80 chromatin remodelling complex},
url = {http://dx.doi.org/10.1038/s41594-017-0003-7},
volume = {25},
year = {2017}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Access to chromatin for processes such as DNA repair and transcription requires the sliding of nucleosomes along DNA. The multi-subunit INO80 chromatin remodelling complex has a particular role in DNA repair. Here we present the cryo electron microscopy structures of the active core complex of human INO80 at 9.6 Å with portions at 4.1 Å resolution along with reconstructions of combinations of subunits. Together these structures reveal the architecture of the INO80 complex, including Ino80 and actin-related proteins, which is assembled around a single Tip49a (RUVBL1) and Tip49b (RUVBL2) AAA+ heterohexamer. An unusual spoked-wheel structural domain of the Ino80 subunit is engulfed by this heterohexamer and the intimate association of this Ino80 domain with the heterohexamer is at  the core of the complex. We also identify a cleft in RUVBL1 and RUVBL2, which forms a major interaction site for partner proteins and likely communicates partner-interactions with its nucleotide binding sites.
AU  - Zhang,X
AU  - Aramayo,RJ
AU  - Willhoft,O
AU  - Ayala,R
AU  - Bythell-Douglas,R
AU  - Wigley,DB
DO  - 10.1038/s41594-017-0003-7
EP  - 44
PY  - 2017///
SN  - 1545-9985
SP  - 37
TI  - CryoEM structures of the human INO80 chromatin remodelling complex
T2  - Nature Structural and Molecular Biology
UR  - http://dx.doi.org/10.1038/s41594-017-0003-7
UR  - https://www.nature.com/articles/s41594-017-0003-7
UR  - http://hdl.handle.net/10044/1/54418
VL  - 25
ER  -
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