Structure and mechanism of the chromatin remodelling factor ISW1a

Kazuhiro Yamada, Timothy D. Frouws, Brigitte Angst, Daniel J. Fitzgerald, Carl DeLuca, Kyoko Schimmele, David F. Sargent and Timothy J. Richmond ()
Additional contact information
Kazuhiro Yamada: ETH Zürich, Institute of Molecular Biology and Biophysics, Schafmattstr. 20
Timothy D. Frouws: ETH Zürich, Institute of Molecular Biology and Biophysics, Schafmattstr. 20
Brigitte Angst: ETH Zürich, Institute of Molecular Biology and Biophysics, Schafmattstr. 20
Daniel J. Fitzgerald: ETH Zürich, Institute of Molecular Biology and Biophysics, Schafmattstr. 20
Carl DeLuca: ETH Zürich, Institute of Molecular Biology and Biophysics, Schafmattstr. 20
Kyoko Schimmele: ETH Zürich, Institute of Molecular Biology and Biophysics, Schafmattstr. 20
David F. Sargent: ETH Zürich, Institute of Molecular Biology and Biophysics, Schafmattstr. 20
Timothy J. Richmond: ETH Zürich, Institute of Molecular Biology and Biophysics, Schafmattstr. 20

Nature, 2011, vol. 472, issue 7344, 448-453

Abstract: Abstract Site-specific recognition of DNA in eukaryotic organisms depends on the arrangement of nucleosomes in chromatin. In the yeast Saccharomyces cerevisiae, ISW1a and related chromatin remodelling factors are implicated in establishing the nucleosome repeat during replication and altering nucleosome position to affect gene activity. Here we have solved the crystal structures of S. cerevisiae ISW1a lacking its ATPase domain both alone and with DNA bound at resolutions of 3.25 Å and 3.60 Å, respectively, and we have visualized two different nucleosome-containing remodelling complexes using cryo-electron microscopy. The composite X-ray and electron microscopy structures combined with site-directed photocrosslinking analyses of these complexes suggest that ISW1a uses a dinucleosome substrate for chromatin remodelling. Results from a remodelling assay corroborate the dinucleosome model. We show how a chromatin remodelling factor could set the spacing between two adjacent nucleosomes acting as a ‘protein ruler’.

Date: 2011
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/nature09947 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:472:y:2011:i:7344:d:10.1038_nature09947

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature09947

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().