Citation

BibTex format

@article{Ayala:2018:10.1038/s41586-018-0021-6,
author = {Ayala, R and Willhoft, O and Aramayo, R and Wilkinson, M and McCormack, E and Ocloo, L and Wigley, D and Zhang, X},
doi = {10.1038/s41586-018-0021-6},
journal = {Nature},
pages = {391--395},
title = {Structure and regulation of the human INO80–nucleosome complex},
url = {http://dx.doi.org/10.1038/s41586-018-0021-6},
volume = {556},
year = {2018}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Access to DNA within nucleosomes is required for a variety of processes in cells including transcription, replication and repair. Consequently, cells encode multiple systems that remodel nucleosomes. These complexes can be simple, involving one or a few protein subunits, or more complicated multi-subunit machines1. Biochemical studies2-4 have placed the motor domains of several remodellers on the superhelical location (SHL) 2 region of the nucleosome. Structural studies on Chd1 and Snf2 (RSC) in complex with nucleosomes5-7 have provided insights into the basic mechanism of nucleosome sliding by these complexes. However, how larger, multi-subunit remodelling complexes, such as INO80, interact with nucleosomes or how remodellers carry out functions such as nucleosome sliding8, histone exchange9, and nucleosome spacing10-12 remains poorly understood. Although some remodellers work as monomers13, others work as highly cooperative dimers11,14,15. Here we present the structure of the INO80 chromatin remodeller with a bound nucleosome revealing that INO80 interacts with nucleosomes in a unique manner with the motor domains located at the entry point to the wrap around the histone core rather than at SHL2. The Arp5-Ies6 module of INO80 makes additional contacts on the opposite side of the nucleosome. This unique arrangement allows the H3 tails of the nucleosome to play a role in regulation, differing from other characterised remodellers.
AU - Ayala,R
AU - Willhoft,O
AU - Aramayo,R
AU - Wilkinson,M
AU - McCormack,E
AU - Ocloo,L
AU - Wigley,D
AU - Zhang,X
DO - 10.1038/s41586-018-0021-6
EP - 395
PY - 2018///
SN - 0028-0836
SP - 391
TI - Structure and regulation of the human INO80–nucleosome complex
T2 - Nature
UR - http://dx.doi.org/10.1038/s41586-018-0021-6
UR - https://www.nature.com/articles/s41586-018-0021-6
UR - http://hdl.handle.net/10044/1/58477
VL - 556
ER -

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