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Biomolecular NMR Assignments

, Volume 12, Issue 1, pp 189–194 | Cite as

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)

  • Harshad Paithankar
  • Pankaj V. Jadhav
  • Amit S. Naglekar
  • Shilpy Sharma
  • Jeetender Chugh
Article
  • 155 Downloads

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.

Keywords

TRBP1 TRBP2 Backbone assignment RNA binding modes NMR spectroscopy 

Notes

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.

Supplementary material

12104_2018_9807_MOESM1_ESM.docx (3 mb)
Supplementary material 1 (DOCX 3062 KB)

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Copyright information

© Springer Science+Business Media B.V., part of Springer Nature 2018

Authors and Affiliations

  1. 1.Department of ChemistryIndian Institute of Science Education & ResearchPuneIndia
  2. 2.Department of BiologyIndian Institute of Science Education & ResearchPuneIndia
  3. 3.Department of BiotechnologySavitrabai Phule Pune University (Formerly University of Pune)PuneIndia

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