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Histone dynamics within the nucleosome octamer play a critical role in SNF2h-mediated nucleosome sliding

By Nathan Gamarra, Geeta J. Narlikar

Posted 16 Mar 2020
bioRxiv DOI: 10.1101/2020.03.14.992073

Elucidating the mechanisms by which ATP-dependent chromatin remodeling enzymes disrupt nucleosome structure is essential to understanding how chromatin states are established and maintained. A key finding informing remodeler mechanism is the observation that the dynamics of protein residues buried within the histone core of the nucleosome are required by specific remodelers to mobilize the nucleosome[1][1]. Recently, a study obtaining cryo-electron microscopy (cryo-EM) structures of remodeler-nucleosome complexes failed to observe stable conformational rearrangements in the histone octamer[2][2]. The authors of this study also failed to replicate the finding that site-specifically restraining histone dynamics inhibits nucleosome sliding by ISWI-family remodelers[2][2]. In contrast, a recent cryo-EM structure detected asymmetric histone dynamics in an ISWI-nucleosome complex[3][3]. Here, using two different protocols, we replicate the original finding in Sinha et al.[1][1] that dynamics within the histone core are required for nucleosome sliding by the human ISWI remodeler, SNF2h. These results firmly establish histone dynamics as an essential feature of ISWI-mediated nucleosome sliding and highlight the care required in designing and performing biochemical experiments investigating nucleosome dynamics. [1]: #ref-1 [2]: #ref-2 [3]: #ref-3

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