Abstract
Human lysyl aminoacyl tRNA synthetase (hLysRS) is integral to a variety of different functions ranging from protein biosynthesis, initiation of a proinflammatory response as well as signal transduction. Another important, non-canonical function of hLysRS is that it chaperones tRNALys,3, the HIV-1 reverse transcription primer molecule into new HIV-1 particles. Since the N-terminal domain of hLysRS has been shown to be essential for such primer uptake, NMR studies of this domain are being conducted to obtain a better understanding of how hLysRS interacts with the primer tRNA. In order to study the RNA binding behavior of this domain, we are studying its complex with a fragment of the cognate tRNA corresponding to the tRNA anticodon loop. We report herein the backbone and side chain NMR resonance assignments of uniformly 15N-, 13C-labeled hLysRS N-terminal domain alone, as well as complexed to RNA.
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Acknowledgments
Professor M. Rance is gratefully acknowledged for assistance with the 3D NMR experiments. The University of Cincinnati College of Medicine NMR Structural Biology Center is also acknowledged for use of their NMR instrumentation, including NIH grants RR19077 and RR027755. Professor K. Greis and the UC Proteomics facility are acknowledged for their assistance with the mass spectrometry. Funding from the University Research Council (PT, SL and AD) is acknowledged.
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Liu, S., Decker, A., Howell, M. et al. 1H, 13C and 15N resonance assignment of the N-terminal domain of human lysyl aminoacyl tRNA synthetase. Biomol NMR Assign 7, 289–292 (2013). https://doi.org/10.1007/s12104-012-9430-x
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DOI: https://doi.org/10.1007/s12104-012-9430-x