Abstract
Plant homeodomains (PHD) and Bromo domains are both chromatin reader domains that recognise histone methylation degree and acetylation state, respectively. The tripartite motif protein TRIM24 is a multidomain protein carrying a PHD-Bromo motif at its C-terminus, through which it is able to bind to histone 3 (H3) N-terminal tails with a specific modification pattern, namely unmethylated at K4 and acetylated at K23 (H3-K4me0K23ac). Here we report the \({}^{1}\hbox {H}, {}^{13}\hbox {C}\) and \({}^{15}\hbox {N}\) backbone resonance assignment of this 23 kDa motif, which we have obtained by heteronuclear multidimensional NMR spectroscopy. Furthermore we show that the secondary \(\hbox {C}_\alpha\) and \(\hbox {C}_\beta\) chemical shifts are in good agreement with a previously published crystal structure.
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We would like to thank Liz Flavell for establishing the protein expression and purification protocols.
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Walser, R., Renshaw, J. & Milbradt, A.G. Backbone resonance assignments for the PHD-Bromo dual-domain of the human chromatin reader TRIM24. Biomol NMR Assign 10, 207–211 (2016). https://doi.org/10.1007/s12104-016-9668-9
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DOI: https://doi.org/10.1007/s12104-016-9668-9