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. 2020 Jul 7;48(15):8332–8348. doi: 10.1093/nar/gkaa552

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© The Author(s) 2020. 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 Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 7. — INO80C is involved in activating cat-3 transcription by mediating the removal of H2A.Z from nucleosomes around cat-3 locus. (A) In-gel assay analysis of the CAT-3 activity levels in WT, ino80^KO and arp8^KO strains. (B) Western blot analyses showing the levels of CAT-3 protein in the WT, ino80^KO and arp8^KO strains. The membranes stained by coomassie blue represent the total protein in each sample and act as loading control for western blot. (C) RT-qPCR assays analyzing the levels of cat-3 mRNA in the WT, ino80^KO and arp8^KO strains. Error bars show s.d. (n = 3). Significance was evaluated by using a two-tailed t-test. ***P < 0.001 versus WT. (D, E) ChIP assays revealing the binding of INO80 (D) and ARP8 (E) at cat-3 locus. (F, G) ChIP assays analyzing the effects of deletion of INO80 (F) and ARP8 (G) on the binding of H2A.Z at cat-3 locus. The H2A.Z^KO strain was used as a negative control. Error bars show s.d. (n = 3). Significance was evaluated by using a two-tailed t-test. **P < 0.01 and ***P < 0.001.