Abstract
TAR RNA binding protein (TRBP) is a double-stranded RNA binding protein involved in various biological processes like cell growth, development, death, etc. The protein exists as two isoforms TRBP2 and TRBP1. TRBP2 contains additional 21 amino acids at its N-terminus, which are proposed to be involved in its membrane localization, when compared to TRBP1. The resonance assignment (19–228) of the double-stranded RNA binding domains (dsRBD 1 and 2) of TRBP2 has been reported earlier. Here, we report 1H, 13C and 15N resonance assignment for dsRBD1 of TRBP2 (1–105) containing the additional N-terminal residues. This assignment will provide deeper insights to understand the effect of these residues on the structure and dynamics of TRBP2 and would therefore help in further elucidating the differences in the role of these isoforms.
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Acknowledgements
Authors thank Prof Jennifer Doudna for the TRBP clones. JC thanks IISER Pune for the start-up grant. JC acknowledges extra mural grant from Department of Science & Technology, India (EMR/2015/001966). SS acknowledges Ramalingaswami fellowship (BT/RLF/Re-entry/11/2012) and SPPU Research and Development grant to Department of Biotechnology. HP thanks IISER Pune for the fellowship; PVJ and ASN acknowledge Department of Biotechnology, India for their Masters in Biotechnology fellowship. Authors thank High-field NMR facility at IISER Pune funded by DST-FIST and IISER Pune.
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Paithankar, H., Jadhav, P.V., Naglekar, A.S. et al. 1H, 13C and 15N resonance assignment of domain 1 of trans-activation response element (TAR) RNA binding protein isoform 1 (TRBP2) and its comparison with that of isoform 2 (TRBP1). Biomol NMR Assign 12, 189–194 (2018). https://doi.org/10.1007/s12104-018-9807-6
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DOI: https://doi.org/10.1007/s12104-018-9807-6