Related ArticlesThe Interaction between tRNA(Lys) 3 and the Primer Activation Signal Deciphered by NMR Spectroscopy.
PLoS One. 2013;8(6):e64700
Authors: Sleiman D, Barraud P, Brachet F, Tisne C
Abstract
The initiation of reverse transcription of the human immunodeficiency virus type 1 (HIV-1) requires the opening of the three-dimensional structure of the primer tRNA(Lys) 3 for its annealing to the viral RNA at the primer binding site (PBS). Despite the fact that the result of this rearrangement is thermodynamically more stable, there is a high-energy barrier that requires the chaperoning activity of the viral nucleocapsid protein. In addition to the nucleotide complementarity to the PBS, several regions of tRNA(Lys) 3 have been described as interacting with the viral genomic RNA. Among these sequences, a sequence of the viral genome called PAS for "primer activation signal" was proposed to interact with the T-arm of tRNA(Lys) 3, this interaction stimulating the initiation of reverse transcription. In this report, we investigate the formation of this additional interaction with NMR spectroscopy, using a simple system composed of the primer tRNA(Lys) 3, the 18 nucleotides of the PBS, the PAS (8 nucleotides) encompassed or not in a hairpin structure, and the nucleocapsid protein. Our NMR study provides molecular evidence of the existence of this interaction and highlights the role of the nucleocapsid protein in promoting this additional RNA-RNA annealing. This study presents the first direct observation at a single base-pair resolution of the PAS/anti-PAS association, which has been proposed to be involved in the chronological regulation of the reverse transcription.
[NMR paper] G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.
G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.
G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.
Biochem J. 2013 Mar 15;450(3):443-57
Authors: Ding X, Zhao X, Watts A
Abstract
GPCRs (G-protein-coupled receptors) are versatile signalling molecules at the cell surface and make up the largest and most diverse family of membrane receptors in the human genome. They convert a large variety of extracellular stimuli into...
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A Primer on LC/NMR/MS
A Primer on LC/NMR/MS
http://www.spectroscopynow.com/common/images/thumbnails/sepspec10145education.jpgIn this primer, Steve Down provides a detailed look at how these analytical techniques have been coupled together to provide an extremely powerful bioanalytical tool.
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[NMR paper] Dynamic activation of protein function: a view emerging from NMR spectroscopy.
Dynamic activation of protein function: a view emerging from NMR spectroscopy.
Related Articles Dynamic activation of protein function: a view emerging from NMR spectroscopy.
Nat Struct Biol. 2001 Nov;8(11):926-31
Authors: Wand AJ
Recent developments in solution NMR methods have allowed for an unprecedented view of protein dynamics. Current insights into the nature of protein dynamics and their potential influence on protein structure, stability and function are reviewed. Particular emphasis is placed on the potential of fast side chain motion...
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11-19-2010 08:44 PM
[NMR paper] Heteronuclear NMR studies of the interaction of tRNA(Lys)3 with HIV-1 nucleocapsid pr
Heteronuclear NMR studies of the interaction of tRNA(Lys)3 with HIV-1 nucleocapsid protein.
Related Articles Heteronuclear NMR studies of the interaction of tRNA(Lys)3 with HIV-1 nucleocapsid protein.
J Mol Biol. 2001 Feb 23;306(3):443-54
Authors: Tisné C, Roques BP, Dardel F
Reverse transcription of HIV-1 viral RNA uses human tRNA(Lys)3 as a primer. Recombinant tRNA(Lys)3 was previously overexpressed in Escherichia coli, 15N-labelled and purified for NMR studies. It was shown to be functional for priming of HIV-1 reverse transcription. Using...
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11-19-2010 08:32 PM
[NMR paper] 19F and 31P NMR spectroscopy of G protein alpha subunits. Mechanism of activation by
19F and 31P NMR spectroscopy of G protein alpha subunits. Mechanism of activation by Al3+ and F-.
Related Articles 19F and 31P NMR spectroscopy of G protein alpha subunits. Mechanism of activation by Al3+ and F-.
J Biol Chem. 1991 Feb 25;266(6):3396-401
Authors: Higashijima T, Graziano MP, Suga H, Kainosho M, Gilman AG
19F and 31P NMR spectroscopy was used to study the mechanism of activation of the alpha subunits of guanine nucleotide-binding regulatory proteins (G proteins) by Al3+, Mg2+, and F-. 19F NMR spectra of solutions containing Al3+,...
The Interaction between tRNA(Lys) 3 and the Primer Activation Signal Deciphered by NMR Spectroscopy.
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