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Reply to: Histone dynamics play a critical role in SNF2h-mediated nucleosome sliding

Nature Structural & Molecular Biology volume 28, pages 552–553 (2021)Cite this article

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The Original Article was published on 05 July 2021

replying to N. Gamarra & G. J. Narlikar Nat. Struct. Mol. Biol. https://doi.org/10.1038/s41594-021-00620-7 (2021)

In our previous study, we proposed a unified mechanism of chromatin remodeling by ISWI family chromatin remodelers, which involves local DNA distortion without notable histone deformation1. The reported high-resolution cryo-electron microscopy (cryo-EM) structures of the ISWI–nucleosome complex showed no obvious histone deformation, and biochemical analyses on crosslinked nucleosomes argued against a strict requirement of histone distortion for chromatin remodeling by yeast Isw1 and its human homolog SNF2H. By contrast, Narlikar and colleagues proposed a critical role for histone deformation in SNF2H-mediated chromatin remodeling2,3.

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Fig. 1: Analyses of the integrity of the H3(L82C)–H4(V81C) octamer.

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References

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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.

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Author notes

  1. Lijuan Yan

    Present address: Boston Children’s Hospital, Boston, MA, USA

Authors and Affiliations

  1. MOE Key Laboratory of Protein Science, Tsinghua University, Beijing, P. R. China

    Lifei Li, Lijuan Yan & Zhucheng Chen

  2. School of Life Science, Tsinghua University, Beijing, P. R. China

    Lifei Li, Lijuan Yan & Zhucheng Chen

  3. Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, Beijing, P. R. China

    Zhucheng Chen

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  1. Lifei Li
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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

Correspondence to Zhucheng Chen.

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The authors declare no competing interests.

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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.

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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.

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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

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