title: Probing the conformation of human tRNA(3)(Lys) in solution by NMR.
abstract: 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.
authors.affiliation: Department of Structural Biology, D105A Fairchild Building, 299 Campus Drive West, Stanford University School of Medicine, Stanford, CA 94305-5126, USA.
authors.forename: Elisabetta Viani
authors.initials: EV
authors.lastname: Puglisi
authors.forename: Joseph D
authors.initials: JD
authors.lastname: Puglisi
mesh_terms: 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
chemical_list: D012346:RNA, Transfer, Amino Acyl; D012996:Solutions; D008274:Magnesium