ArticleBiopolymers2012
Comparison of solution conformations and stabilities of modified helix 69 rRNA analogs from bacteria and human.
Article in Biopolymers, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- 16S rRNA methyltransferase KsgA contributes to oxidative stress and antibiotic resistance in Pseudomonas aeruginosa.Scientific reports · 2024Article
- Article
- Article
- Regulation and Function of RNA Pseudouridylation in Human Cells.Annual review of genetics · 2020Review
- Computational and NMR studies of RNA duplexes with an internal pseudouridine-adenosine base pair.Scientific reports · 2019Article
- Pseudouridine modifications influence binding of aminoglycosides to helix 69 of bacterial ribosomes.Organic & biomolecular chemistry · 2017Article
- Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly.Nature structural & molecular biology · 2015Article
- Structure modulation of helix 69 from Escherichia coli 23S ribosomal RNA by pseudouridylations.Nucleic acids research · 2014Article
- The contribution of pseudouridine to stabilities and structure of RNAs.Nucleic acids research · 2014Article
- Pseudouridine: still mysterious, but never a fake (uridine)!RNA biology · 2014Review
- Selection of heptapeptides that bind helix 69 of bacterial 23S ribosomal RNA.Bioorganic & medicinal chemistry · 2013Article
- Ligand- and pH-induced conformational changes of RNA domain helix 69 revealed by 2-aminopurine fluorescence.Angewandte Chemie (International ed. in English) · 2012Article
- Modulation of conformational changes in helix 69 mutants by pseudouridine modifications.Biophysical chemistryArticle
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The helix 69 (H69) region of the large subunit (28S) ribosomal RNA (rRNA) of Homo sapiens contains five pseudouridine (Ψ) residues out of 19 total nucleotides, three of which are highly conserved. In this study, the effects of this abundant modified nucleotide on the structure and stability of H69 were compared with those of uridine in double-stranded (stem) regions. These results were compared with previous hairpin (stem plus single-stranded loop) studies to understand the contributions of the loop sequences to H69 structure and stability. The role of a loop nucleotide substitution from an A in bacteria (position 1918 in Escherichia coli 23S rRNA) to a G in eukaryotes (position 3734 in H. sapiens 28S rRNA) was examined. Thermodynamic parameters for the duplex RNAs were obtained through UV melting studies, and differences in the modified and unmodified RNA structures were examined by circular dichroism spectroscopy. The overall folded structure of human H69 appears to be similar to the bacterial RNA, consistent with the idea that ribosome structure and function are highly conserved; however, our results reveal subtle differences in structure and stability between the bacterial and human H69 RNAs in both the stem and loop regions. These findings may be significant with respect to H69 as a potential drug target site.
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