Mechanism of DNA translocation underlying chromatin remodelling by Snf2

Meijing Li, Xian Xia, Yuanyuan Tian, Qi Jia, Xiaoyu Liu, Ying Lu, Ming Li (), Xueming Li () and Zhucheng Chen ()
Additional contact information
Meijing Li: Tsinghua University
Xian Xia: Tsinghua University
Yuanyuan Tian: Tsinghua University
Qi Jia: Chinese Academy of Sciences
Xiaoyu Liu: Tsinghua University
Ying Lu: Chinese Academy of Sciences
Ming Li: Chinese Academy of Sciences
Xueming Li: Tsinghua University
Zhucheng Chen: Tsinghua University

Nature, 2019, vol. 567, issue 7748, 409-413

Abstract: Abstract Chromatin remodellers include diverse enzymes with distinct biological functions, but nucleosome-sliding activity appears to be a common theme1,2. Among the remodelling enzymes, Snf2 serves as the prototype to study the action of this protein family. Snf2 and related enzymes share two conserved RecA-like lobes3, which by themselves are able to couple ATP hydrolysis to chromatin remodelling. The mechanism by which these enzymes couple ATP hydrolysis to translocate the nucleosome along the DNA remains unclear2,4–8. Here we report the structures of Saccharomyces cerevisiae Snf2 bound to the nucleosome in the presence of ADP and ADP-BeFx. Snf2 in the ADP-bound state adopts an open conformation similar to that in the apo state, and induces a one-base-pair DNA bulge at superhelix location 2 (SHL2), with the tracking strand showing greater distortion than the guide strand. The DNA distortion propagates to the proximal end, leading to staggered translocation of the two strands. The binding of ADP-BeFx triggers a closed conformation of the enzyme, resetting the nucleosome to a relaxed state. Snf2 shows altered interactions with the DNA in different nucleotide states, providing the structural basis for DNA translocation. Together, our findings suggest a fundamental mechanism for the DNA translocation that underlies chromatin remodelling.

Date: 2019
References: Add references at CitEc
Citations: View citations in EconPapers (6)

Downloads: (external link)
https://www.nature.com/articles/s41586-019-1029-2 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:567:y:2019:i:7748:d:10.1038_s41586-019-1029-2

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

DOI: 10.1038/s41586-019-1029-2

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 ().