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. 2017 Oct 13;8:928. doi: 10.1038/s41467-017-00988-5

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/..

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Fig. 7 — Downregulation of Nt-acetylation of histone H4 facilitates nuclear accumulation of CK2α and its binding to histone H4 in lung cancer cells. a Representative confocal scanning images of CK2α localization in Scr and H1299 cells (left panel). The staining intensity of CK2α was quantified by software ImageJ from NIH (right diagram). Scale bars, 5 μm. Results are shown as mean ± s.d. from more than 30 cells from three independent experiments; two-tailed Student’s t-test, **P < 0.01 compared with the Scr control. b Western blot analysis of CK2α distribution in scrambled and NatD-KD H1299 cells with indicated antibodies. N nucleus, C cytoplasm. c Peptide pulldown assay to detect the interaction between H4 (1–31) or H3 (1–20) peptide (pNt-ac-H4, pH4, pH4S1A, or pH3) and CK2α in H1299 cell nuclear extracts (top panel). Equal peptide biotinylated on C terminus is shown by dot blot analysis with streptavidin (middle panel). Nt-ac-H4 was confirmed by dot blot analysis with anti-Nt-ac-H4 antibody (bottom panel). d SDS-PAGE analysis of purified recombinant CK2α (1–335) from E. coli stained by Coomassie brilliant blue (CBB). MW: protein molecular weight markers. e MST assay to identify direct interactions between CK2α (1–335) and H4 or Nt-ac-H4 peptide. The dissociation constant (K _D) between CK2α (1–335) and H4 peptide is 33.5 ± 2.67 μΜ. f ChIP analysis of the enrichment of CK2α on the Slug promoter in Scr and NatD-KD H1299 cells. IgG served as a negative control. Results are shown as mean ± s.d. from three independent experiments; two-tailed Student’s t-test, **P < 0.01 compared with the indicated control. g Quantitative real-time PCR analysis of mRNA levels of CK2α and Slug normalized to GAPDH in Scr and NatD-KD H1299 cells in the absence or presence of siRNA to CK2α. NC, siRNA mimics negative control. Data are mean ± s.d. of three independent experiments; Student’s t-test, *P < 0.05, **P < 0.01 compared with the indicated control. h Western blot analysis of indicated proteins from Scr and NatD-KD H1299 cells in the absence or presence of siRNA to CK2α. GAPDH served as a loading control