This is a preview of subscription content, access via your institution
Access options
Access Nature and 54 other Nature Portfolio journals
Get Nature+, our best-value online-access subscription
$29.99 / 30 days
cancel any time
Subscribe to this journal
Receive 12 print issues and online access
$189.00 per year
only $15.75 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Data availability
Source data are provided with this paper.
References
Yan, L., Wu, H., Li, X., Gao, N. & Chen, Z. Structures of the ISWI–nucleosome complex reveal a conserved mechanism of chromatin remodeling. Nat. Struct. Mol. Biol. 26, 258–266 (2019).
Sinha, K. K., Gross, J. D. & Narlikar, G. J. Distortion of histone octamer core promotes nucleosome mobilization by a chromatin remodeler. Science 355, eaaa3761 (2017).
Gamarra, N. & Narlikar, G. J. Histone dynamics play a critical role in SNF2h-mediated nucleosome sliding. Nat. Struct. Mol. Biol. https://doi.org/10.1038/s41594-021-00620-7 (2021).
Glaeser, R. M. Proteins, interfaces, and cryo-EM grids. Curr. Opin. Colloid Interface Sci. 34, 1–8 (2018).
Armache, J. P. et al. Cryo-EM structures of remodeler-nucleosome intermediates suggest allosteric control through the nucleosome. Elife 8, e46057 (2019).
Bazett-Jones, D. P., Côté, J., Landel, C. C., Peterson, C. L. & Workman, J. L. The SWI/SNF complex creates loop domains in DNA and polynucleosome arrays and can disrupt DNA-histone contacts within these domains. Mol. Cell. Biol. 19, 1470–1478 (1999).
Boyer, L. A., Shao, X., Ebright, R. H. & Peterson, C. L. Roles of the histone H2A-H2B dimers and the (H3-H4)2 tetramer in nucleosome remodeling by the SWI-SNF complex. J. Biol. Chem. 275, 11545–11552 (2000).
Kassabov, S. R., Zhang, B., Persinger, J. & Bartholomew, B. SWI/SNF unwraps, slides, and rewraps the nucleosome. Mol. Cell 11, 391–403 (2003).
Acknowledgements
We thank Y. Tian for helping with the nucleosome centering assays. This study was supported by the National Key Research and Development Program (2019YFA0508902 and 2017YFA0102900 to Z.C.); the National Natural Science Foundation of China (31825016 to Z.C.); and the Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences.
Author information
Authors and Affiliations
Contributions
L.L. performed the experiments and L.L., L.Y. and Z.C. analyzed the results. Z.C. wrote the manuscript with help from the other authors.
Corresponding author
Ethics declarations
Competing interests
The authors declare no competing interests.
Additional information
Peer review information Anke Sparmann was the primary editor on this article and managed its editorial process and peer review in collaboration with the rest of the editorial team.
Publisher’s note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Extended data
Extended Data Fig. 1 Remodeling activities of the crosslinked and reduced nucleosomes.
(a) Non-reducing SDS-PAGE analysis of the crosslinked (X) and reduced forms of the H3L82C/H4V81C octamer. Treatment of the crosslinked nucleosome with 100 mM DTT at 37 °C for 1 h and at 55 °C for 2 h resulted in reversion of ~25% and ~50% of the samples into the reduced form. (b) Nucleosome centering activities of the wild type (WT), crosslinked (X) and crosslinked and then reduced by DTT at 37 °C for 1 h (X + DTT) samples. Error bars indicate s.d. of the means (n = 3 independent experiments). Representative gels are shown below. The sliding rate constants are indicated. (c) Nucleosome centering activities of the WT, crosslinked (X) and crosslinked and then reduced by DTT at 55 °C for 2 h (X + DTT) samples.
Supplementary information
Supplementary Information
Supplementary Note 1.
Source data
Source Data Fig. 1
Source images.
Source Data Extended Data Fig. 1
Source images.
Rights and permissions
About this article
Cite this article
Li, L., Yan, L. & Chen, Z. Reply to: Histone dynamics play a critical role in SNF2h-mediated nucleosome sliding. Nat Struct Mol Biol 28, 552–553 (2021). https://doi.org/10.1038/s41594-021-00621-6
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1038/s41594-021-00621-6
This article is cited by
-
Histone dynamics play a critical role in SNF2h-mediated nucleosome sliding
Nature Structural & Molecular Biology (2021)