ArticleRNA (New York, N.Y.)2007
Characterization of a cyanobacterial RNase P ribozyme recognition motif in the IRES of foot-and-mouth disease virus reveals a unique structural element.
Article in RNA (New York, N.Y.), 2007. 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, 35 citations in OpenAlex.
- Insights into Structural and Mechanistic Features of Viral IRES Elements.Frontiers in microbiology · 2017Review
- Viral tRNA Mimicry from a Biocommunicative Perspective.Frontiers in microbiology · 2017Review
- Geneticin Stabilizes the Open Conformation of the 5' Region of Hepatitis C Virus RNA and Inhibits Viral Replication.Antimicrobial agents and chemotherapy · 2016Article
- Analysis of the interaction between host factor Sam68 and viral elements during foot-and-mouth disease virus infections.Virology journal · 2015Article
- Messenger RNAs bearing tRNA-like features exemplified by interferon alfa 5 mRNA.Cellular and molecular life sciences : CMLS · 2015Article
- Discovery of rosavirus 2, a novel variant of a rodent-associated picornavirus, in children from The Gambia.Virology · 2014Article
- Role of RNA structure motifs in IRES-dependent translation initiation of the coxsackievirus B3: new insights for developing live-attenuated strains for vaccines and gene therapy.Molecular biotechnology · 2013Review
- Candidate RNA structures for domain 3 of the foot-and-mouth-disease virus internal ribosome entry site.Nucleic acids research · 2013Article
- RNA structural elements of hepatitis C virus controlling viral RNA translation and the implications for viral pathogenesis.Viruses · 2012Review
- Alternative Mechanisms to Initiate Translation in Eukaryotic mRNAs.Comparative and functional genomics · 2012Article
- Pr77 and L1TcRz: A dual system within the 5'-end of L1Tc retrotransposon, internal promoter and HDV-like ribozyme.Mobile genetic elements · 2012Article
- Comparative complete genome analysis of Indian type A foot-and-mouth disease virus field isolates.Virus genes · 2011Article
- Identification of an hepatitis delta virus-like ribozyme at the mRNA 5'-end of the L1Tc retrotransposon from Trypanosoma cruzi.Nucleic acids research · 2011Article
- Tailoring the switch from IRES-dependent to 5'-end-dependent translation with the RNase P ribozyme.RNA (New York, N.Y.) · 2010Article
- Insights into the biology of IRES elements through riboproteomic approaches.Journal of biomedicine & biotechnology · 2010Review
- Comparative analysis of the large fragment of the 5' untranslated region (LF-5' UTR) of serotype A foot-and-mouth disease virus field isolates from India.Virus genes · 2009Article
- Viral IRES RNA structures and ribosome interactions.Trends in biochemical sciences · 2008Review
- The impact of RNA structure on picornavirus IRES activity.Trends in microbiology · 2008Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Translation initiation driven by internal ribosome entry site (IRES) elements is dependent on the structural organization of the IRES region. Picornavirus IRES are organized in structural domains, in which the terminal stem-loops participate in functional RNA-protein interactions. However, the mechanistic role performed by the central domain during internal initiation has not been elucidated yet. Here we show that the foot-and-mouth-disease virus IRES contains a structural motif that serves in vitro as substrate for the Synechocystis sp. RNase P ribozyme, a structure-dependent endonuclease that participates in tRNA precursor processing. Recognition of the IRES substrate was dose dependent, required high magnesium concentration, and resulted in the formation of cleavage products with 5' phosphate and 3' hydroxyl ends. Mapping of the core recognition motif indicated that it overlapped with the apical region of the central domain. Two IRES constructs containing nucleotide substitutions in the apical region of the central domain that reorganized RNA structure displayed an altered pattern of cleavage by the cyanobacterial ribozyme generating new cleavage events in nearby residues. From these data it is inferred that the central domain of the IRES region has evolved a tRNA structural mimicry that renders it a substrate for RNase P ribozyme reaction. Recognition of this motif was affected in defective IRES mutants with a local RNA structure reorganization, suggesting that its structural preservation is required for IRES activity.
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