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Biomol NMR Assign. 2016 Apr;10(1):207-11. doi: 10.1007/s12104-016-9668-9. Epub 2016 Feb 15.

Backbone resonance assignments for the PHD-Bromo dual-domain of the human chromatin reader TRIM24.

Author information

1
Structure and Biophysics, AstraZeneca Discovery Sciences, Alderley Park, SK10 4TG, United Kingdom. Reto.Walser@astrazeneca.com.
2
RAD, AstraZeneca Discovery Sciences, Alderley Park, SK10 4TG, United Kingdom.
3
Structure and Biophysics, AstraZeneca Discovery Sciences, Alderley Park, SK10 4TG, United Kingdom.

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 1H, 13C and 15N backbone resonance assignment of this 23 kDa motif, which we have obtained by heteronuclear multidimensional NMR spectroscopy. Furthermore we show that the secondary Cα and Cβ chemical shifts are in good agreement with a previously published crystal structure.

KEYWORDS:

Backbone assignment; Bromo domain; PHD domain; TRIM24

PMID:
26878853
DOI:
10.1007/s12104-016-9668-9
[Indexed for MEDLINE]

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