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. 2022 Sep 26;50(18):10376–10384. doi: 10.1093/nar/gkac790

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© The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 4. — Streptavidin association with H2A N-tail domains does not inhibit RSC remodeling-dependent nucleosome DNA site exposure. (A). Detection of RSC remodeling-dependent exposure of the HhaI cognate DNA site at the nucleosome dyad, which can be uncoupled to mobilization (35). (B). Experimental timeline. HhaI and RSC were added at t = 0 and t = 6 min., respectively. Samples of the digest were taken at the times indicated by the black arrows below the line. (C, D). Products of digestion were run on 5% SDS PAGE gels and quantified by phosphorimagery. (D). Plot of average percent uncut vs time (min). Streptavidin bound and unbound samples are indicated by the open and filled squares, respectively (n = 3, avg. SD 4%).