Abstract
Human TATA binding protein associated factor 2 N (TAF15) is a RNA/DNA binding protein involved in many aspects of RNA and DNA metabolism. TAF15 contains an N-terminal transcriptional activation domain and C-terminal region comprising the RNA recognition motif (RRM) and RanBP2 type zinc finger domains with interspersed RGG motifs. In this study we report the complete backbone and side chain resonance assignments of human TAF15-RRM and backbone assignments of TAF15-RRM-RanBP2.
Similar content being viewed by others
References
Baechtold H, Kuroda M, Sok J, Ron D, Lopez BS, Akhmedov AT (1999) Human 75-kDa DNA-pairing protein is identical to the pro-oncoprotein TLS/FUS and is able to promote D-loop formation. J Biol Chem 274:34337–34342
Bertolotti A, Bell B, Tora L (1999) The N-terminal domain of human TAFII68 displays transactivation and oncogenic properties. Oncogene 18:8000–8010
Hoell JI, Larsson E, Runge S, Nusbaum JD, Duggimpudi S, Farazi TA et al (2011) RNA targets of wild-type and mutant FET family proteins. Nat Struct Mol Biol 18:1428–1431
Ibrahim F, Maragkakis M, Alexiou P, Maronski MA, Dichter MA, Mourelatos Z (2013) Identification of in vivo, conserved, TAF15 RNA binding sites reveals the impact of TAF15 on the neuronal transcriptome. Cell Rep 3:301–308
Iko Y, Kodama TS, Kasai N, Oyama T, Morita EH, Muto T et al (2004) Domain architectures and characterization of an RNA-binding protein, TLS. J Biol Chem 279:44834–44840
Keller R (2004) The Computer Aided Resonance Assignment Tutorial. 1st edn. ISBN 3-85600- 112-3, CANTINA Verlag
Liu X, Niu C, Ren J, Zhang J, Xie X, Zhu H et al (2013) The RRM domain of human fused in sarcoma protein reveals a non-canonical nucleic acid binding site. Biochim Biophys Acta 1832:375–385
Nguyen CD, Mansfield RE, Leung W, Vaz PM, Loughlin FE, Grant RP et al (2011) Characterization of a family of RanBP2-type zinc fingers that can recognize single-stranded RNA. J Mol Biol 407:273–283
Tan AY, Manley JL (2009) The TET family of proteins: functions and roles in disease. J Mol Cell Biol 1:82–92
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
Acknowledgments
We thank Department of Biotechnology (DBT), Government of India for providing financial support for the High Field NMR spectrometers at the ICGEB, New Delhi and NII, New Delhi. MK is a recipient of Indian Council for medical Research (ICMR) senior research fellowship. AKG is a recipient of Department of Biotechnology senior research fellowship. This study is supported by grant to NSB from the Department of Science and Technology (DST), Government of India and ICGEB core funds.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Kashyap, M., Ganguly, A.K. & Bhavesh, N.S. Sequence-specific resonance assignments of human TAF15-RRM and TAF15-RRM-RanBP2. Biomol NMR Assign 9, 103–106 (2015). https://doi.org/10.1007/s12104-014-9553-3
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s12104-014-9553-3