Probing the conformation of human tRNA(3)(Lys) in solution by NMR.
Human tRNA(3)(Lys) acts as a primer for the reverse transcription of human immunodeficiency virus genomic RNA. To form an initiation complex with genomic RNA, tRNA(3)(Lys) must reorganize its secondary structure. To provide a starting point for mechanistic studies of the formation of the initiation complex, we here present solution NMR investigations of human tRNA(3)(Lys). We use a straightforward set of NMR experiments to show that tRNA(3)(Lys) adopts a standard transfer ribonucleic acid tertiary structure in solution, and that Mg(2+) is required for this folding. The results underscore the power of NMR to reveal rapidly the conformation of RNAs.
Puglisi
Elisabetta Viani
EV
Department of Structural Biology, D105A Fairchild Building, 299 Campus Drive West, Stanford University School of Medicine, Stanford, CA 94305-5126, USA.
Puglisi
Joseph D
JD
D001483:Base Sequence; D006801:Humans; D008274:Magnesium / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D009690:Nucleic Acid Conformation; D012346:RNA, Transfer, Amino Acyl / Q000737:chemistry* / Q000378:metabolism; D012996:Solutions
D012346:RNA, Transfer, Amino Acyl; D012996:Solutions; D008274:Magnesium