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1H, 15N and 13C backbone and side chain resonance assignments of the RRM domain from human RBM24

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Abstract

Tissue development requires the expression of a regulated subset of genes, and it is becoming clear that the process of alternative splicing also plays an important role in the production of necessary tissue-specific isoforms. However, only a few of these tissue-specific splicing factors in mammals have so far been discovered. One of these factors is the RNA-binding protein RBM24 which has been recently identified as a major regulator of alternative splicing in cardiac and skeletal muscle development. The RBM24 protein contains an RNA recognition motif (RRM) domain that presumably mediates the binding to target pre-mRNA required for regulation of the splicing patterns. Here we report 1H, 15N and 13C chemical shift assignments of the backbone and sidechain atoms for the RRM domain from human RBM24. Secondary chemical shift analysis and relaxation measurement confirm the canonical architecture of the RRM domain. The data will allow for atomic level studies aimed at understanding splicing regulation of target genes in heart and muscle development and investigation into a separate role of RBM24 in modulating mRNA stability of genes involved in the p53 tumor suppressor pathway.

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References

  • Amrane S, Rebora K, Zniber I, Dupuy D, Mackereth CD (2014) Backbone-independent nucleic acid binding by splicing factor SUP-12 reveals key aspects of molecular recognition. Nat Commun 5:4595

    Article  ADS  Google Scholar 

  • 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 6:277–293

    Article  Google Scholar 

  • Fetka I, Radeghieri A, Bouwmeester T (2000) Expression of the RNA recognition motif-containing protein SEB-4 during Xenopus embryonic development. Mech Dev 94:283–286

    Article  Google Scholar 

  • Grifone R, Xie X, Bourgeois A, Saquet A, Duprez D, Shi D-L (2014) The RNA-binding protein Rbm24 is transiently expressed in myoblasts and is required for myogenic differentiation during vertebrate development. Mech Dev 134:1–15

    Article  Google Scholar 

  • Jiang Y, Zhang M, Qian Y, Xu E, Zhang J, Chen X (2014) Rbm24, an RNA-binding protein and a target of p53, regulates p21 expression via mRNA stability. J Biol Chem 289:3164–3175

    Article  Google Scholar 

  • Kong SW, Hu YW, Ho JWK, Ikeda S, Polster S, John R, Hall JL, Bisping E, Pieske B, dos Remedios CG, Pu WT (2010) Heart failure-associated changes in RNA splicing of sarcomere genes. Circ Cardiovasc Genet 3:138–146

    Article  Google Scholar 

  • Kuwasako K, Takahashi M, Unzai S, Tsuda K, Yoshikawa S, He F, Kobayashi N, Güntert P, Shirouzu M, Ito T, Tanaka A, Yokoyama S, Hagiwara M, Kuroyanagi H, Muto Y (2014) RBFOX and SUP-12 sandwich a G base to cooperatively regulate tissue-specific splicing. Nat Struct Mol Biol 21:778–786

    Article  Google Scholar 

  • Li HY, Bourdelas A, Carron C, Shi DL (2010) The RNA-binding protein Seb4/RBM24 is a direct target of MyoD and is required for myogenesis during Xenopus early development. Mech Dev 127:281–291

    Article  Google Scholar 

  • Maragh S, Miller RA, Bessling SL, McGaughey DM, Wessels MW, de Graaf B, Stone EA, Bertoli-Avella AM, Gearhart JD, Fisher S, McCallion AS (2011) Identification of RNA binding motif proteins essential for cardiovascular development. BMC Dev Biol 11:62

    Article  Google Scholar 

  • Maragh S, Miller RA, Bessling SL, Wang G, Hook PW, McCallion AS (2014) Rbm24a and Rbm24b are required for normal somitogenesis. PLoS ONE 9:e105460

    Article  ADS  Google Scholar 

  • Miyamoto S, Hidaka K, Jin D, Morisaki T (2009) RNA-binding proteins Rbm38 and Rbm24 regulate myogenic differentiation via p21-dependent and -independent regulatory pathways. Genes Cells 14:1241–1252

    Article  Google Scholar 

  • Poon KL, Tan KT, Wei YY, Ng CP, Colman A, Korzh V, Xu XQ (2012) RNA-binding protein RBM24 is required for sarcomere assembly and heart contractility. Cardiovasc Res 94:418–427

    Article  Google Scholar 

  • Senn H, Werner B, Messerle BA, Weber C, Traber R, Wüthrich K (1989) Stereospecific assignment of the methyl 1H NMR lines of valine and leucine in polypeptides by nonrandom 13C labelling. FEBS Lett 249:113–118

    Article  Google Scholar 

  • Shen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44:213–223

    Article  Google Scholar 

  • Tamiola K, Acar B, Mulder FA (2010) Sequence-specific random coil chemical shifts of intrinsically disordered proteins. J Am Chem Soc 132:18000–18003

    Article  Google Scholar 

  • Xu E, Zhang J, Zhang M, Jiang Y, Cho SJ, Chen X (2014) RNA-binding protein RBM24 regulates p63 expression via mRNA stability. Mol Cancer Res 12:359–369

    Article  Google Scholar 

  • Yang J, Hung L-H, Licht T, Kostin S, Looso M, Khrameeva E, Bindereif A, Schneider A, Braun T (2014) RBM24 is a major regulator of muscle-specific alternative splicing. Dev Cell 31:87–99

    Article  Google Scholar 

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Acknowledgments

This work was supported by grants from the Department of Science and Technology (DST), Government of India. SKU is a recipient of the DST INSPIRE Faculty award [IFA-13 CH-102].

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Correspondence to Santosh Kumar Upadhyay.

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Upadhyay, S.K., Mackereth, C.D. 1H, 15N and 13C backbone and side chain resonance assignments of the RRM domain from human RBM24. Biomol NMR Assign 10, 237–240 (2016). https://doi.org/10.1007/s12104-016-9674-y

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  • DOI: https://doi.org/10.1007/s12104-016-9674-y

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