Abstract
Human ribonuclease 4 (RNase 4) is the most evolutionarily conserved member of the 8 canonical human pancreatic-like RNases, showing more than 90 % identity with bovine and porcine homologues. The enzyme displays ribonucleolytic activity with a strong preference for uracil-containing RNA substrates, a feature only shared with human eosinophil derived-neurotoxin (EDN, or RNase 2) and eosinophil cationic protein (ECP, or RNase 3). It is also the shortest member of the human family, with a significantly truncated C-terminal tail. Its unique active-site pocket and high degree of conservation among vertebrates suggest that the enzyme plays a crucial biological function. Here, we report on the 1H, 13C and 15N backbone resonance assignments of RNase 4, providing means to characterize its molecular function at the atomic level by NMR.
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Acknowledgements
This work was supported by a Natural Sciences and Engineering Research Council of Canada (NSERC) Discovery grant (RGPIN 402623-2011), and a “Fonds de Recherche Québec-Santé” (FRQS) Research Scholar Junior 1 Career Award (to N.D). D.G. is the recipient of an NSERC Alexander Graham Bell Canada Graduate Scholarship (Ph.D.). The authors would like to thank Tara Sprules and Sameer Al-Abdul-Wahid from the Québec/Eastern Canada High Field NMR Facility for excellent NMR technical assistance.
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Gagné, D., Doucet, N. Sequence-specific backbone 1H, 13C, and 15N resonance assignments of human ribonuclease 4. Biomol NMR Assign 9, 181–185 (2015). https://doi.org/10.1007/s12104-014-9570-2
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DOI: https://doi.org/10.1007/s12104-014-9570-2