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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.
The authors declare no competing interests.
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.
(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
Nature Structural & Molecular Biology (2021)