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Fig. 1 | Epigenetics & Chromatin

Fig. 1

From: The histone and non-histone methyllysine reader activities of the UHRF1 tandem Tudor domain are dispensable for the propagation of aberrant DNA methylation patterning in cancer cells

Fig. 1

LIG1K126me2 is read by a high-affinity interaction through the UHRF1 TTD. a Protein reader domain microarrays consisting of 308 GST-tagged domains (see Additional file 1: Fig. S1), each printed in duplicate, were probed by either anti-GST antibody, or Cy3-labeled LIG1(118–130)K126me2, H3(1–20)K9me2, or LIG1(118–130)K126me0 (left). Reader arrays were quantified using ArrayNinja software. Data were normalized to the brightest signal for each peptide (right). Error bars represent the range from duplicate spots. Full reader array datasets are available in Additional file 2: Table S1. b The indicated GST-tagged reader domains were hybridized to histone peptide microarrays at 1 µM, followed by fluorescent detection and quantified by ArrayNinja. Results for interactions with H3(1–20)K9me2 and LIG1(118–130)K126me2 are shown. Error bars represent standard error of the mean of six printed spots. Full histone peptide array data are available in Additional file 3: Table S2. c Fluorescence polarization binding assays between the indicated GST-tagged reader domains and either FAM-LIG1(118–130)K126me2 (left) or H3(1–20)K9me2-FAM (right). Error bars represent the 95% confidence interval from triplicate measurements

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