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

Overview of attention for article published in Nature, June 2014
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About this Attention Score

  • In the top 25% of all research outputs scored by Altmetric
  • High Attention Score compared to outputs of the same age (81st percentile)

Mentioned by

twitter
10 tweeters
wikipedia
2 Wikipedia pages

Citations

dimensions_citation
66 Dimensions

Readers on

mendeley
227 Mendeley
citeulike
3 CiteULike
Title
Histone H4 tail mediates allosteric regulation of nucleosome remodelling by linker DNA
Published in
Nature, June 2014
DOI 10.1038/nature13380
Pubmed ID
Authors

William L. Hwang, Sebastian Deindl, Bryan T. Harada, Xiaowei Zhuang

Abstract

Imitation switch (ISWI)-family remodelling enzymes regulate access to genomic DNA by mobilizing nucleosomes. These ATP-dependent chromatin remodellers promote heterochromatin formation and transcriptional silencing by generating regularly spaced nucleosome arrays. The nucleosome-spacing activity arises from the dependence of nucleosome translocation on the length of extranucleosomal linker DNA, but the underlying mechanism remains unclear. Here we study nucleosome remodelling by human ATP-dependent chromatin assembly and remodelling factor (ACF), an ISWI enzyme comprising a catalytic subunit, Snf2h, and an accessory subunit, Acf1 (refs 2, 11 - 13). We find 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, abolishes the linker-length sensitivity in remodelling. Addition of exogenous H4-tail peptide or deletion of the nucleosomal H4 tail also diminishes the linker-length sensitivity. Moreover, Acf1 binds both the H4-tail peptide and DNA in an amino (N)-terminal domain dependent manner, and in the ACF-bound nucleosome, lengthening the linker DNA reduces the Acf1-H4 tail proximity. Deletion of the N-terminal portion of Acf1 (or its homologue in yeast) abolishes linker-length sensitivity in remodelling and leads 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.

Twitter Demographics

The data shown below were collected from the profiles of 10 tweeters who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 227 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 8 4%
Germany 2 <1%
United Kingdom 2 <1%
Russia 1 <1%
France 1 <1%
Spain 1 <1%
Japan 1 <1%
Mexico 1 <1%
Unknown 210 93%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 74 33%
Researcher 49 22%
Student > Bachelor 21 9%
Student > Master 15 7%
Other 14 6%
Other 36 16%
Unknown 18 8%
Readers by discipline Count As %
Agricultural and Biological Sciences 115 51%
Biochemistry, Genetics and Molecular Biology 67 30%
Chemistry 9 4%
Medicine and Dentistry 5 2%
Physics and Astronomy 3 1%
Other 10 4%
Unknown 18 8%

Attention Score in Context

This research output has an Altmetric Attention Score of 7. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 25 November 2016.
All research outputs
#3,327,640
of 18,605,513 outputs
Outputs from Nature
#47,268
of 82,183 outputs
Outputs of similar age
#35,065
of 196,687 outputs
Outputs of similar age from Nature
#708
of 991 outputs
Altmetric has tracked 18,605,513 research outputs across all sources so far. Compared to these this one has done well and is in the 81st percentile: it's in the top 25% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 82,183 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 92.3. This one is in the 41st percentile – i.e., 41% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 196,687 tracked outputs that were published within six weeks on either side of this one in any source. This one has done well, scoring higher than 81% of its contemporaries.
We're also able to compare this research output to 991 others from the same source and published within six weeks on either side of this one. This one is in the 28th percentile – i.e., 28% of its contemporaries scored the same or lower than it.