Abstract
Heterogeneous nuclear ribonucleoproteins (hnRNPs) can be divided into subgroups based on their RNA-binding characteristics. One subgroup in mammalian cells are the Poly(C)-binding proteins (PCBPs) comprised of hnRNP K/J and hnRNP E1-4 [the latter also known as PCBP 1–4 or α-complex proteins (α-CP) 1–4]. Each subgroup member has three K homology (KH) nucleic acid-binding domains. Individual KH domains bind short single-stranded (ss), poly-pyrimidine-rich nucleic acid sequences with rather weak affinity. In this study, we report the 1H, 13C and 15N backbone resonance assignments of the first and second KH domains of hnRNP E1, which plays a pivotal role in posttranscriptional and translational regulation of RNA targets. Our NMR assignments lay the foundation for a detailed investigation of the dynamic cooperation of the tandem KH1 and KH2 domains to bind nucleic acids.
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Acknowledgments
This work was supported by the South Carolina Clinical & Translational Research (SCTR) Institute (UL1TR000062). We thank Dr. Daniella Ishimaru (MUSC) for KH1–KH2 NMR sample preparation and acknowledge Dr. Philip H. Howe (MUSC) for the generous gift of the parent GST-hnRNP E1 construct and the support of the Hollings Marine Laboratory NMR facility for this work.
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Li, Y., Hennig, M. 1H, 15N and 13C backbone resonance assignments of the N-terminal, tandem KH domains of human hnRNP E1. Biomol NMR Assign 9, 431–434 (2015). https://doi.org/10.1007/s12104-015-9624-0
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DOI: https://doi.org/10.1007/s12104-015-9624-0