Abstract
Human lysyl aminoacyl tRNA synthetase (hLysRS) is a multi-functional aminoacyl tRNA synthetase which is primarily involved in protein biosynthesis as well as crucial processes ranging from proinflammatory response to signal transduction. One important, non-canonical function of hLysRS is to target tRNALys,3, the HIV-1 reverse transcription primer molecule, for uptake and packaging into new HIV-1 particles. Since the anticodon binding (ACB) domain of hLysRS is required for proper recognition of its cognate tRNA, NMR studies of the ACB domain are being conducted to enhance our understanding of how hLysRS interacts with these RNAs during protein biosysnthesis as well as HIV-1 viral packaging. Here, we report the backbone and side chain NMR resonance assignments of the uniformly 15N-, 13C-labeled ACB domain of hLysRS.
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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) and NSF REU 0754114 (JOM) are acknowledged.
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Liu, S., Howell, M., Melby, J. et al. 1H, 13C and 15N resonance assignment of the anticodon binding domain of human lysyl aminoacyl tRNA synthetase. Biomol NMR Assign 6, 173–176 (2012). https://doi.org/10.1007/s12104-011-9349-7
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DOI: https://doi.org/10.1007/s12104-011-9349-7