NDLI: Histone H4 tail mediates allosteric regulation of nucleosome remodelling by linker DNA

Content Provider	PubMed Central
Author	Hwang, William L. Sebastian, Deindl Harada, Bryan T. Zhuang, Xiaowei
Abstract	ISWI-family remodelling enzymes regulate access to genomic DNA by mobilizing nucleosomes 1 . These ATP-dependent chromatin remodellers promote heterochromatin formation and transcriptional silencing 1 by generating regularly-spaced nucleosome arrays 2-5 . The nucleosome-spacing activity arises from regulation of nucleosome translocation by the length of extranucleosomal linker DNA 6-10 , but the underlying mechanism remains unclear. Here, we studied nucleosome remodelling by human ACF, an ISWI enzyme comprised of a catalytic subunit, Snf2h, and an accessory subunit, Acf1 2,11-13 . We found that ACF senses linker DNA length through an interplay between its accessory and catalytic subunits mediated by the histone H4 tail of the nucleosome. Mutation of AutoN, an auto-inhibitory domain within Snf2h that bears sequence homology to the H4 tail 14 , abolished the linker-length sensitivity in remodelling. Addition of exogenous H4-tail peptide or deletion of the nucleosomal H4 tail also diminished the linker-length sensitivity. Moreover, the accessory subunit Acf1 bound the H4-tail peptide and DNA in a manner that depended on its N-terminal domain, and lengthening the linker DNA in the nucleosome reduced the proximity between Acf1 and the H4 tail. Deletion of the N-terminal portion of Acf1 (or its homologue in yeast) abolished linker-length sensitivity in nucleosome remodeling and led to severe growth defects in vivo. Taken together, our results suggest a mechanism for nucleosome spacing where linker DNA sensing by Acf1 is allosterically transmitted to Snf2h through the H4 tail of the nucleosome. For nucleosomes with short linker DNA, Acf1 preferentially binds to the H4 tail, allowing AutoN to inhibit the ATPase activity of Snf2h. As the linker DNA lengthens, Acf1 shifts its binding preference to the linker DNA, freeing the H4 tail to compete AutoN off the ATPase and thereby activating ACF.
Related Links	http://dx.doi.org/10.1038/nature13380
Ending Page	217
Page Count	5
Starting Page	213
File Format	PDF
ISSN	00280836
e-ISSN	14764687
Journal	Nature
Issue Number	7513
Volume Number	512
Language	English
Publisher Date	2014-06-01
Access Restriction	Open
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

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