Biomolecular NMR Assignments

, Volume 4, Issue 2, pp 143–145 | Cite as

1H, 13C and 15N NMR assignments of RNA recognizing motifs 1 and 2 of BRUNOL-3 protein from human involved in myotonic dystrophy

  • Harshesh Bhatt
  • Maruthi Kashyap
  • Neel Sarovar BhaveshEmail author


BRUNOL-3 protein, an alternate splicing factor, has been known for playing a major role in myotonic dystrophy. It binds to the cTNT m-RNA and prevents splicing of exon-5 region, leading to translation of troponin protein having differential affinity for Ca2+. Here, we report sequence-specific 1H, 13C, and 15N resonance assignments for RNA recognition motifs 1 and 2 of BRUNOL-3 protein.


BRUNOL-3 Myotonic dystrophy Cardiac troponin T Alternate splicing factor 



The work is funded by Department of Science and technology, Government of India under SERC FAST Track scheme vide diary no 100/IFD/5657/2009-2010. We thank Dr. Nicolas Charlet-Berguerand, IGBMC, University of Strasbourg, France for construct of BRUNOL-3. We thank Department of Biotechnology, Government of India for providing financial support for the High Field NMR spectrometers at the ICGEB, New Delhi and NII, New Delhi. We thank Prof. Virander S. Chauhan for his interest and support. Mr. Alok Sharma is acknowledged for his help during installation of the NMR at ICGEB. HB is a recipient of Council for Scientific and Industrial Research (CSIR) junior research fellowship. MK is a recipient of Indian Council for Medical Research (ICMR) junior research fellowship.


  1. Bhavesh NS, Panchal SC, Hosur RV (2001) An efficient high-throughput resonance assignment procedure for structural genomics and protein folding research by NMR. Biochemistry 40:14727–14735CrossRefGoogle Scholar
  2. Charlet-B N, Singh G, Logan PE, Cooper TA (2002) Dynamic antagonism between CELF proteins and PTB regulate splicing of a muscle-specific exon in both muscle and nonmuscle cells. Mol Cell 9:649–658CrossRefGoogle Scholar
  3. Findeisen M, Brand T, Berger S (2006) A 1H-NMR thermometer suitable for cryoprobes. Magn Reson Chem 45:175–178CrossRefGoogle Scholar
  4. Keller R (2004) The computer aided resonance assignment tutorial, 1st edn. ISBN 3-85600-112-3, CANTINA VerlagGoogle Scholar
  5. Korade-Mirnics Z, Babitzke P, Hoffman E (1998) Myotonic dystrophy: molecular windows on a complex etiology. Nucleic Acids Res 26:1363–1368CrossRefGoogle Scholar
  6. Ladd AN, Charlet-B N, Cooper TA (2001) The CELF family of RNA binding proteins is implicated in cell-specific and developmentally regulated alternative splicing. Mol Cell Biol 21:1285–1296CrossRefGoogle Scholar
  7. Lu X, Timchenko NA, Timchenko LT (1999) Cardiac elav-type RNA-binding protein (ETR-3) binds to RNA CUG repeats expanded in myotonic dystrophy. Hum Mol Genet 8:53–60CrossRefGoogle Scholar
  8. Singh G, Charlet-B N, Han J, Cooper TA (2004) ETR-3 and CELF4 protein domains required for RNA binding and splicing activity in vivo. Nucleic Acids Res 32:1232–1241CrossRefGoogle Scholar
  9. Tsilfidis C, MacKenzie AE, Mettler G, Barcelo J, Korneluk RG (1992) Correlation between CTG trinucleotide repeats length and frequency of severe congenital myotonic dystrophy. Nat Genet 1:192–195CrossRefGoogle Scholar
  10. 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 4:171–180CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  • Harshesh Bhatt
    • 1
  • Maruthi Kashyap
    • 1
  • Neel Sarovar Bhavesh
    • 1
    Email author
  1. 1.Structural and Computational Biology GroupInternational Center for Genetic Engineering and BiotechnologyNew DelhiIndia

Personalised recommendations