ArticleNucleic acids research2010
Dissecting the role of conserved box C/D sRNA sequences in di-sRNP assembly and function.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Conservation of Archaeal C/D Box sRNA-Guided RNA Modifications.Frontiers in microbiology · 2021Review
- Small, Smaller, Smallest: Minimal Structural Requirements for a Fully Functional Box C/D Modification Guide RNA.Biomolecules · 2019Article
- Biology and clinical relevance of noncoding sno/scaRNAs.Trends in cardiovascular medicine · 2018Review
- Unusual C΄/D΄ motifs enable box C/D snoRNPs to modify multiple sites in the same rRNA target region.Nucleic acids research · 2017Article
- Box C/D sRNA stem ends act as stabilizing anchors for box C/D di-sRNPs.Nucleic acids research · 2016Article
- Box C/D guide RNAs recognize a maximum of 10 nt of substrates.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Ribosome biogenesis in the yeast Saccharomyces cerevisiae.Genetics · 2013Review
- Ribonucleoproteins in archaeal pre-rRNA processing and modification.Archaea (Vancouver, B.C.) · 2013Review
- The box C/D sRNP dimeric architecture is conserved across domain Archaea.RNA (New York, N.Y.) · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
In all three kingdoms of life, nucleotides in ribosomal RNA (rRNA) are post-transcriptionally modified. One type of chemical modification is 2'-O-ribose methylation, which is, in eukaryotes and archaea, performed by box C/D small ribonucleoproteins (box C/D sRNPs in archaea) and box C/D small nucleolar ribonucleoproteins (box C/D snoRNPs in eukaryotes), respectively. Recently, the first structure of any catalytically active box C/D s(no)RNP determined by electron microscopy and single particle analysis surprisingly demonstrated that they are dimeric RNPs. Mutational analyses of the Nop5 protein interface suggested that di-sRNP formation is also required for the in vitro catalytic activity. We have now analyzed the functional relevance of the second interface, the sRNA interface, within the box C/D di-sRNP. Mutations in conserved sequence elements of the sRNA, which allow sRNP assembly but which severely interfere with the catalytic activity of box C/D sRNPs, prevent formation of the di-sRNP. In addition, we can observe the dimeric box C/D sRNP architecture with a different box C/D sRNP, suggesting that this architecture is conserved. Together, these results provide further support for the functional relevance of the di-sRNP architecture and also provide a structural explanation for the observed defects in catalysis of 2'-O-ribose methylation.
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