Cross-talk within a functional INO80 complex dimer regulates nucleosome sliding
- Imperial College London, United Kingdom
Abstract
Several chromatin remodellers have the ability to space nucleosomes on DNA. For ISWI remodellers, this involves an interplay between H4 histone tails, the AutoN and NegC motifs of the motor domains that together regulate ATPase activity and sense the length of DNA flanking the nucleosome. By contrast, the INO80 complex also spaces nucleosomes but is not regulated by H4 tails and lacks the AutoN and NegC motifs. Instead nucleosome sliding requires cooperativity between two INO80 complexes that monitor DNA length simultaneously on either side of the nucleosome during sliding. The C-terminal domain of the human Ino80 subunit (Ino80CTD) binds cooperatively to DNA and dimerisation of these domains provides crosstalk between complexes. ATPase activity, rather than being regulated, instead gradually becomes uncoupled as nucleosome sliding reaches an end point and this is controlled by the Ino80CTD. A single active ATPase motor within the dimer is sufficient for sliding.
Article and author information
Author details
Funding
Cancer Research UK (C6913/A21608)
- Dale B Wigley
Wellcome (095519/Z/11/Z)
- Dale B Wigley
Wellcome (098412/Z/12/Z)
- Xiaodong Zhang
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
Copyright
© 2017, Willhoft et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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Cross-talk within a functional INO80 complex dimer regulates nucleosome sliding
eLife 6:e25782.
https://doi.org/10.7554/eLife.25782
