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. 2020 Sep 1;9:e58675. doi: 10.7554/eLife.58675

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© 2020, Dong et al

This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.

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Figure 3. — (A, B) In vitro GST pull-down assays using GST-tagged PHF1-Tudor proteins and histones prepared from H3t-expressed HEK293T cells. GST proteins from input, bound, and unbound flow-through (FT) fractions were analyzed using SDS-PAGE with Coomassie Brilliant Blue (CBB) staining (A). Input and bound histones were analyzed using western blotting with indicated antibodies (B). (C) MS/MS spectrum of the histone H3t peptide corresponding to residues 19–36. The observed y and b ions and fragment map are shown. (D) Spectral counts of methylated lysine residues in input or pull-down fractions. Control histones (Input) or pooled histones pulled-down with the GST-PHF1-Tudor (pull-down) were digested with LysN proteinase and subjected to LC-MS/MS analysis (detected peptides were summarized in Supplementary file 1). The spectral counts of methylated lysine residues in each fraction are shown. Since short peptides cleaved at unmodified lysine residues could not be efficiently detected in the LC-MS/MS analysis, these data do not accurately reflect their abundance.