1993
DOI: 10.1021/bi00055a015
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Abstract: A 25-nucleotide RNA with the sequence of the trans-activation response (TAR) element of equine infectious anemia virus (EIAV) was analyzed by biochemical methods and by one- and two-dimensional NMR spectroscopy. NMR, nuclease probing, and polyacrylamide gel migration rates show that the RNA consists of an A-helical stem capped by two non-Watson-Crick U-G base pairs and a compact four-nucleotide loop. The loop is stabilized by base stacking, with loop nucleotides C12 and C15 stacked upon U11 and G16, respective… Show more

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Cited by 20 publications
(17 citation statements)
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References 49 publications
(51 reference statements)
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“…The repetition delay was 15 s and the results showed that except for H2 protons of adenine residues most proton T 1 values were less than 2.17 s (the null point was less than 1.5 s). This result is consistent with that reported by Hoffman et al (1993) for an NMR study of an RNA structure. 2D proton NMR spectra were collected in HzO and D20.…”
Section: D and 2d Nmr Experimentssupporting
confidence: 93%
“…The repetition delay was 15 s and the results showed that except for H2 protons of adenine residues most proton T 1 values were less than 2.17 s (the null point was less than 1.5 s). This result is consistent with that reported by Hoffman et al (1993) for an NMR study of an RNA structure. 2D proton NMR spectra were collected in HzO and D20.…”
Section: D and 2d Nmr Experimentssupporting
confidence: 93%
“…It binds to the functional TAR region in the LTR, increases the efficiency of viral gene transcription, and consequently plays an important role in the regulation of viral gene expression [40][41][42]. There are three predicted functional regions in the S2 protein, the nucleoporin motif, the SH3 domain binding motif, and the nuclear localization sequence.…”
Section: Discussionmentioning
confidence: 99%
“…High quality NMR spectra have been obtained for this complex between the folded protein domain and a non double-helical nucleic acid structure. With the exception of the investigation of the hnRNP C-rU8 complex , NMR studies of RNA-protein recognition have hitherto been limited to the individual RNA Hoffman et al, 1993;Jaeger and Tinoco, 1993;Wimberly et al, 1993) or protein (Hoffman et al, 1991;Wittekind et al, 1992) components, or to small peptides in complex with oligonucleotides (Puglisi et al, 1992(Puglisi et al, , 1993. This study demonstrates that NMR can be used to investigate the recognition of structured RNAs by folded protein domains, without the need to reduce either the protein or the RNA to its minimal recognition elements.…”
Section: Discussionmentioning
confidence: 99%