Abstract
1H, 13C and 15N resonance assignments are presented for the first bromo domain of TbBDF5 (TbBDF5-bromo1) from Trypanosoma brucei. TbBDF5 is localized in the nucleus and plays a potential role in transcription regulation. Bromo domains can recognize acetylated histone through a conserved binding pocket. Here we report the NMR resonance assignments of TbBDF5-bromo1 domain for further studies of the relationship between its structure and function.
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Data availability
The chemical shift data have been deposited in the BioMagResBank (http://www.bmrb.wisc.edu) with Accession Number 51357.
References
Alonso VL, Tavernelli LE, Pezza A, Cribb P, Ritagliati C, Serra E (2019) Aim for the readers! bromodomains as new targets against Chagas’ disease. Curr Med Chem 26:6544–6563
Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277293
Filippakopoulos P, Picaud S, Mangos M, Keates T, Lambert JP, Barsyte-Lovejoy D, Felletar I, Volkmer R, Müller S, Pawson T, Gingras AC, Arrowsmith CH, Knapp S (2012) Histone recognition and large-scale structural analysis of the human bromodomain family. Cell 149:214–231
Fleck K, Nitz M, Jeffers V (2021) “Reading” a new chapter in protozoan parasite transcriptional regulation. PLoS Pathog 17:e1010056
Fujisawa T, Filippakopoulos P (2017) Functions of bromodomain-containing proteins and their roles in homeostasis and cancer. Nat Rev Mol Cell Biol 18:246–262
Goddard TD, Kneller DG (1993) SPARKY3. University of California, San Francisco
Marmorstein R, Berger SL (2001) Structure and function of bromodomains in chromatin-regulating complexes. Gene 272:1–9
Schulz D, Mugnier MR, Paulsen EM, Kim HS, Chung CW, Tough DF, Rioja I, Prinjha RK, Papavasiliou FN, Debler EW (2015) Bromodomain proteins contribute to maintenance of bloodstream form stage identity in the african trypanosome. PLoS Biol 13:e1002316
Staneva DP, Carloni R, Auchynnikava T, Tong P, Rappsilber J, Jeyaprakash AA, Matthews KR, Allshire RC (2021) A systematic analysis of Trypanosoma brucei chromatin factors identifies novel protein interaction networks associated with sites of transcription initiation and termination. Genome Res 31:2138–2154
Wishart DS, Sykes BD (1994) The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4:171–180
Zeng L, Zhou MM (2002) Bromodomain: an acetyl-lysine binding domain. FEBS Lett 513:124–128
Acknowledgements
We thank F. Delaglio and A. Bax for providing NMRPipe and NMRDraw and also thank Goddard and Kneller for providing SPARKY software. This work was supported by the Chinese National Natural Science Foundation (Grant Numbers 32071220 and 31500601).
Funding
The Funder was funded by the Chinese National Natural Science Foundation (Grant Numbers 32071220 and 31500601).
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Yang, L., Zhang, X., Zhang, J. et al. 1H, 13C and 15N resonance assignments of TbBDF5-bromo1 domain from Trypanosoma brucei. Biomol NMR Assign 16, 253–255 (2022). https://doi.org/10.1007/s12104-022-10088-1
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DOI: https://doi.org/10.1007/s12104-022-10088-1