Abstract
Human antigen R (HuR) is a ubiquitous protein that recognizes adenylate and uridylate-rich elements in mRNA, thereby interfering with the fate of protein translation. This protein plays a central role in the outcome of the inflammatory response as it may stabilize or silence mRNAs of key components of the immune system. HuR is able to interact with other RNA-binding proteins, reflecting a complex network that dictates mRNAs post-transcriptional control. HuR is composed of three functional domains, known as RNA-recognition motifs (RRM1, RRM2 and RRM3). It is known that RRM1 is the most important domain for mRNA-binding affinity. In this study, we completed the NMR chemical shift assignment of the RRM1 domain of HuR, as a first step to further establishing the structure, dynamics and function relationship for this protein.
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Acknowledgments
This work was supported by grants from Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ) and by a Brazil Initiative Collaboration grant from Brown University to A. S. P. A. M. and C. L. are recipients of a Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) graduate fellowship.
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The authors declare that they have no conflict of interest.
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Mujo, A., Lixa, C., Carneiro, L.A.M. et al. 1H, 15N and 13C resonance assignments of the RRM1 domain of the key post-transcriptional regulator HuR. Biomol NMR Assign 9, 281–284 (2015). https://doi.org/10.1007/s12104-014-9592-9
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DOI: https://doi.org/10.1007/s12104-014-9592-9