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. 2018 Nov 1;9:4574. doi: 10.1038/s41467-018-07072-6

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© The Author(s) 2018

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. 2 — Engineering the Taf14-YEATS-based reader of H3K9cr. a Surface view of the Taf14-YEATS G82A mutant structure in the apo-state. The side chains of W81, A82, and F62 are shown as green sticks. b Structural overlay of the acyllysine-binding site in the Taf14-YEATS:H3K9bu (lavender/orange) complex and the apo state of Taf14-YEATS G82A (green). c Superimposed ¹H,¹⁵N HSQC spectra of uniformly ¹⁵N-labeled G82A mutant of Taf14-YEATS recorded while the indicated peptides were added stepwise. The spectra are color coded according to the protein:peptide molar ratio. d Binding curves used to determine K_d of taf14-YEATS G82A by tryptophan fluorescence. e Real-time qPCR analysis of various transcripts in the wild-type strain, TAF14 delete strain, and taf14 mutant strains. The mean ± SD are calculated from three biological replicates