ArticleNucleic acids research2005
Characterizing the function and structural organization of the 5' tRNA-like motif within the hepatitis C virus quasispecies.
Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed.
- Review
- 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
- LOOP IIId of the HCV IRES is essential for the structural rearrangement of the 40S-HCV IRES complex.Nucleic acids research · 2016Article
- Exploiting tRNAs to Boost Virulence.Life (Basel, Switzerland) · 2016Review
- Messenger RNAs bearing tRNA-like features exemplified by interferon alfa 5 mRNA.Cellular and molecular life sciences : CMLS · 2015Article
- Inhibition of hepatitis C virus by an M1GS ribozyme derived from the catalytic RNA subunit of Escherichia coli RNase P.Virology journal · 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
- 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
- Tailoring the switch from IRES-dependent to 5'-end-dependent translation with the RNase P ribozyme.RNA (New York, N.Y.) · 2010Article
- Viral IRES RNA structures and ribosome interactions.Trends in biochemical sciences · 2008Review
- Inhibition of no tail (ntl) gene expression in zebrafish by external guide sequence (EGS) technique.Molecular biology reports · 2008Article
- The impact of RNA structure on picornavirus IRES activity.Trends in microbiology · 2008Article
- A method for in vitro assembly of hepatitis C virus core protein and for screening of inhibitors.Analytical biochemistry · 2007Article
- Characterization of a cyanobacterial RNase P ribozyme recognition motif in the IRES of foot-and-mouth disease virus reveals a unique structural element.RNA (New York, N.Y.) · 2007Article
- Accurate energies of hydrogen bonded nucleic acid base pairs and triplets in tRNA tertiary interactions.Nucleic acids research · 2006Article
- RNase III cleavage demonstrates a long range RNA: RNA duplex element flanking the hepatitis C virus internal ribosome entry site.Nucleic acids research · 2005Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hepatitis C virus (HCV) RNA is recognized and cleaved in vitro by RNase P enzyme near the AUG start codon. Because RNase P identifies transfer RNA (tRNA) precursors, it has been proposed that HCV RNA adopts structural similarities to tRNA. Here, we present experimental evidence of RNase P sensitivity conservation in natural RNA variant sequences, including a mutant sequence (A368-G) selected in vitro because it presented changes in the RNA structure of the relevant motif. The variation did not abrogate the original RNase P cleavage, but instead, it allowed a second cleavage at least 10 times more efficient, 4 nt downstream from the original one. The minimal RNA fragment that confers sensitivity to human RNase P enzyme was located between positions 299 and 408 (110 nt). Therefore, most of the tRNA-like domain resides within the viral internal ribosome entry site (IRES) element. In the variant, in which the mutation stabilizes a 4 nt stem-loop, the second cleavage required a shorter (60 nt) substrate, internal to the minimal fragment substrate, conforming a second tRNA-like structure with similarities to a 'Russian-doll' toy. This new structure did not impair IRES activity, albeit slightly reduced the efficiency of translation both in vitro and in transfected cells. Conservation of the original tRNA-like conformation together with preservation of IRES activity points to an essential role for this motif. This conservation is compatible with the presence of RNA structures with different complexity around the AUG start codon within a single viral population (quasispecies).
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.