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1H, 13C, and 15N backbone and sidechain chemical shift assignments for the HEAT2 domain of human eIF4GI

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Abstract

The translation initiation factor eIF4G is required for the translation of many eukaryotic messenger RNAs. Its interaction with the ATP-dependent RNA helicase eIF4A plays an important role in the regulation of translation initiation. eIF4G in humans and other higher eukaryotes contains three HEAT domains, of which HEAT1 and HEAT2 contain binding sites for eIF4A. Here we report the near complete NMR resonance assignment of the 192-residue HEAT2 domain of the human translation initiation factor eIF4GI. The chemical shift data constitute the basis for NMR structural studies aimed at expanding understanding of the role of interactions between the initiation factor eIF4A and eIF4G in translation initiation.

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References

  • Bellsolell L, Cho-Park PF, Poulin F, Sonenberg N, Burley SK (2006) Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1. Structure 14:913–923

    Article  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. doi:10.1007/BF00197809

    Article  Google Scholar 

  • Gal M, Edmonds KA, Milbradt AG, Takeuchi K, Wagner G (2011) Speeding up direct 15N detection: hCaN 2D NMR experiment. J Biomol NMR 51:497–504. doi:10.1007/s10858-011-9580-7

    Article  Google Scholar 

  • Goto NK, Gardner KH, Mueller GA, Willis RC, Kay LE (1999) A robust and cost-effective method for the production of Val, Leu, Ile (δ1) methyl-protonated 15N-, 13C-, 2H-labeled proteins. J Biomol NMR 13:369–374

    Article  Google Scholar 

  • Keller RLJ (2004) The computer aided resonance assignment tutorial. Cantina, Goldau

    Google Scholar 

  • Marintchev A, Edmonds KA, Marintcheva B, Hendrickson E, Oberer M, Suzuki C, Herdy B, Sonenberg N, Wagner G (2009) Topology and regulation of the human eIF4A/4G/4H helicase complex in translation initiation. Cell 136:447–460. doi:10.1016/j.cell.2009.01.014

    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. doi:10.1007/s10858-009-9333-z

    Article  Google Scholar 

  • Goddard TD, Kneller DG SPARKY 3. University of California, San Francisco

  • Yamazaki T, Forman-Kay JD, Kay LE (1993) Two-dimensional NMR experiments for correlating 13Cβ and 1Hδ/ε chemical shifts of aromatic residues in 13C-labeled proteins via scalar couplings. J Am Chem Soc 23:11054–11055

    Article  Google Scholar 

Download references

Acknowledgments

This research was supported by NIH Grants CA68262, GM047467 and EB002026. Instrumentation used for this research was purchased with support from NIH grants GM066360 and 1S10RR10219015. We thank Assen Marintchev for helpful discussions.

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Correspondence to Gerhard Wagner.

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Edmonds, K.A., Wagner, G. 1H, 13C, and 15N backbone and sidechain chemical shift assignments for the HEAT2 domain of human eIF4GI. Biomol NMR Assign 9, 157–160 (2015). https://doi.org/10.1007/s12104-014-9564-0

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  • DOI: https://doi.org/10.1007/s12104-014-9564-0

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