¹H, ¹³C and ¹⁵N resonance assignment of the N-terminal domain of human lysyl aminoacyl tRNA synthetase.
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 tRNA(Lys,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 (15)N-, (13)C-labeled hLysRS N-terminal domain alone, as well as complexed to RNA.
Department of Chemistry, University of Cincinnati, 301 Clifton Court, Cincinnati, OH 45221-0172, USA.
Sheng
S
Liu
Aaron
A
Decker
Mike
M
Howell
Carol
C
Caperelli
Pearl
P
Tsang
D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D006801:Humans; D008250:Lysine-tRNA Ligase / Q000737:chemistry*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011522:Protons
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons; D008250:Lysine-tRNA Ligase