ArticleNucleic acids research2000
The box C/D motif directs snoRNA 5'-cap hypermethylation.
Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Decoding the molecular script of 2'-O-ribomethylation: Implications across CNS disorders.Heliyon · 2024Review
- Subverting the Canon: Novel Cancer-Promoting Functions and Mechanisms for snoRNAs.International journal of molecular sciences · 2024Review
- sRNAfrag: a pipeline and suite of tools to analyze fragmentation in small RNA sequencing data.Briefings in bioinformatics · 2023Article
- Dysregulation of Small Nucleolar RNAs in B-Cell Malignancies.Biomedicines · 2022Review
- Anomalous HIV-1 RNA, How Cap-Methylation Segregates Viral Transcripts by Form and Function.Viruses · 2022Review
- A SnoRNA-derived piRNA interacts with human interleukin-4 pre-mRNA and induces its decay in nuclear exosomes.Nucleic acids research · 2015Article
- Widespread RNA 3'-end oligouridylation in mammals.RNA (New York, N.Y.) · 2012Article
- Requirement of rRNA methylation for 80S ribosome assembly on a cohort of cellular internal ribosome entry sites.Molecular and cellular biology · 2011Article
- The divergent eukaryote Trichomonas vaginalis has an m7G cap methyltransferase capable of a single N2 methylation.Nucleic acids research · 2008Article
- Evolutionary conservation supports ancient origin for Nudt16, a nuclear-localized, RNA-binding, RNA-decapping enzyme.Nucleic acids research · 2008Article
- Spliceosomal snRNAs in the unicellular eukaryote Trichomonas vaginalis are structurally conserved but lack a 5'-cap structure.RNA (New York, N.Y.) · 2008Article
- Systematic identification of non-coding RNA 2,2,7-trimethylguanosine cap structures in Caenorhabditis elegans.BMC molecular biology · 2007Article
- Biochemical and genetic analysis of RNA cap guanine-N2 methyltransferases from Giardia lamblia and Schizosaccharomyces pombe.Nucleic acids research · 2007Article
- Role of pre-rRNA base pairing and 80S complex formation in subnucleolar localization of the U3 snoRNP.Molecular and cellular biology · 2004Article
- A structural, phylogenetic, and functional study of 15.5-kD/Snu13 protein binding on U3 small nucleolar RNA.RNA (New York, N.Y.) · 2003Article
- The product of the survival of motor neuron (SMN) gene is a human telomerase-associated protein.Molecular biology of the cell · 2002Article
- Small nucleolar RNAs: versatile trans-acting molecules of ancient evolutionary origin.Gene expression · 2002Review
- A well-connected and conserved nucleoplasmic helicase is required for production of box C/D and H/ACA snoRNAs and localization of snoRNP proteins.Molecular and cellular biology · 2001Article
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Authors and funding
3 authors.
Funding
Abstract
The 5'-cap structure of most spliceosomal small nuclear RNAs (snRNAs) and certain small nucleolar RNAs (snoRNAs) undergoes hypermethylation from a 7-methylguanosine to a 2,2, 7-trimethylguanosine structure. 5'-Cap hypermethylation of snRNAs is dependent upon a conserved sequence element known as the Sm site common to most snRNAs. Here we have performed a mutational analysis of U3 and U14 to determine the cis-acting sequences required for 5'-cap hypermethylation of Box C/D snoRNAs. We have found that both the conserved sequence elements Box C (termed C' in U3) and Box D are necessary for cap hypermethylation. Furthermore, the terminal stem structure that is formed by sequences that flank Box C (C' in U3) and Box D is also required. However, mutation of other conserved sequences has no effect on hypermethylation of the cap. Finally, the analysis of fragments of U3 and U14 RNAs indicates that the Box C/D motif, including Box C (C' in U3), Box D and the terminal stem, is capable of directing cap hypermethylation. Thus, the Box C/D motif, which is important for snoRNA processing, stability, nuclear retention, protein binding, nucleolar localization and function, is also necessary and sufficient for cap hypermethylation of these RNAs.
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