ArticleBiochemistry2008
X-ray structures of U2 snRNA-branchpoint duplexes containing conserved pseudouridines.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 41 citations in OpenAlex.
- U2 snRNP recognizes the branch site through a loaded-spring strand-invasion mechanism.Nucleic acids research · 2026Article
- Structural and dynamic effects of pseudouridine modifications on noncanonical interactions in RNA.RNA (New York, N.Y.) · 2023Article
- The plant epitranscriptome: revisiting pseudouridine and 2'-O-methyl RNA modifications.Plant biotechnology journal · 2022Review
- Computational and NMR studies of RNA duplexes with an internal pseudouridine-adenosine base pair.Scientific reports · 2019Article
- Structural and functional modularity of the U2 snRNP in pre-mRNA splicing.Critical reviews in biochemistry and molecular biology · 2019Review
- Pseudouridines on Trypanosoma brucei spliceosomal small nuclear RNAs and their implication for RNA and protein interactions.Nucleic acids research · 2019Article
- Dynamic stacking of an expected branch point adenosine in duplexes containing pseudouridine-modified or unmodified U2 snRNA sites.Biochemical and biophysical research communications · 2019Article
- Review
- Noncanonical registers and base pairs in human 5' splice-site selection.Nucleic acids research · 2016Article
- An atlas of RNA base pairs involving modified nucleobases with optimal geometries and accurate energies.Nucleic acids research · 2015Article
- Insight into the mechanisms and functions of spliceosomal snRNA pseudouridylation.World journal of biological chemistry · 2014Review
- Pseudouridine: still mysterious, but never a fake (uridine)!RNA biology · 2014Review
- Structural basis of lariat RNA recognition by the intron debranching enzyme Dbr1.Nucleic acids research · 2014Article
- RNA pseudouridylation: new insights into an old modification.Trends in biochemical sciences · 2013Review
- Impact of base pair identity 5' to the spliceosomal branch site adenosine on branch site conformation.RNA (New York, N.Y.) · 2012Article
- Widespread recognition of 5' splice sites by noncanonical base-pairing to U1 snRNA involving bulged nucleotides.Genes & development · 2012Article
- Pseudouridines in spliceosomal snRNAs.Protein & cell · 2011Review
- Structural model of the p14/SF3b155 · branch duplex complex.RNA (New York, N.Y.) · 2011Article
- Effect of pseudouridylation on the structure and activity of the catalytically essential P6.1 hairpin in human telomerase RNA.Nucleic acids research · 2010Article
- Invariant U2 snRNA nucleotides form a stem loop to recognize the intron early in splicing.Molecular cell · 2010Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
A pseudouridine-modified region of the U2 small nuclear (sn)RNA anneals with the intronic branchpoint sequence and positions a bulged adenosine to serve as the nucleophile in the first chemical step of pre-mRNA splicing. We have determined three X-ray structures of RNA oligonucleotides containing the pseudouridylated U2 snRNA and the branchpoint consensus sequences. The expected adenosine branchpoint is extrahelical in a 1.65 A resolution structure containing the mammalian consensus sequence variant and in a 2.10 A resolution structure containing a shortened Saccharomyces cerevisiae consensus sequence. The adenosine adjacent to the expected branchpoint is extrahelical in a third structure, which contains the intact yeast consensus sequence at 1.57 A resolution. The hydration and base stacking interactions mediated by the U2 snRNA pseudouridines correlate with the identity of the unpaired adenosine. The expected adenosine bulge is associated with a well-stacked pseudouridine, which is linked via an ordered water molecule to a neighboring nucleotide. In contrast, the bulge of the adjacent adenosine shifts the base stacking and disrupts the water-mediated interactions of the pseudouridine. These structural differences may contribute to the ability of the pseudouridine modification to promote the bulged conformation of the branch site adenosine and to enhance catalysis by snRNAs. Furthermore, iodide binding sites are identified adjacent to the unconventional bulged adenosine, and the structure of the mammalian consensus sequence variant provides a high-resolution view of a hydrated magnesium ion bound in a similar manner to a divalent cation binding site of the group II intron.
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Registered trials
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