ArticleRNA (New York, N.Y.)2000
Complementarity between the mRNA 5' untranslated region and 18S ribosomal RNA can inhibit translation.
Article in RNA (New York, N.Y.), 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- Poly(G)RNA biology · 2024Article
- C3P3-G1: first generation of a eukaryotic artificial cytoplasmic expression system.Nucleic acids research · 2019Article
- Article
- Expression of distinct maternal and somatic 5.8S, 18S, and 28S rRNA types during zebrafish development.RNA (New York, N.Y.) · 2017Article
- Structures of yeast 80S ribosome-tRNA complexes in the rotated and nonrotated conformations.Structure (London, England : 1993) · 2014Article
- An evolutionary conserved pattern of 18S rRNA sequence complementarity to mRNA 5' UTRs and its implications for eukaryotic gene translation regulation.Nucleic acids research · 2013Article
- Translation termination efficiency modulates ATF4 response by regulating ATF4 mRNA translation at 5' short ORFs.Nucleic acids research · 2012Article
- Broad-specificity mRNA-rRNA complementarity in efficient protein translation.PLoS genetics · 2012Article
- Searching for IRES.RNA (New York, N.Y.) · 2006Review
- Internal ribosome entry site structural motifs conserved among mammalian fibroblast growth factor 1 alternatively spliced mRNAs.Molecular and cellular biology · 2004Article
- ARC-1, a sequence element complementary to an internal 18S rRNA segment, enhances translation efficiency in plants when present in the leader or intercistronic region of mRNAs.Nucleic acids research · 2004Article
- The ribosome filter hypothesis.Proceedings of the National Academy of Sciences of the United States of America · 2002Review
- The 5' and 3' extremities of the satellite tobacco necrosis virus translational enhancer domain contribute differentially to stimulation of translation.RNA (New York, N.Y.) · 2002Article
- Structure and function of a cap-independent translation element that functions in either the 3' or the 5' untranslated region.RNA (New York, N.Y.) · 2000Article
- Antizyme expression: a subversion of triplet decoding, which is remarkably conserved by evolution, is a sensor for an autoregulatory circuit.Nucleic acids research · 2000Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In eubacteria, base pairing between the 3' end of 16S rRNA and the ribosome-binding site of mRNA is required for efficient initiation of translation. An interaction between the 18S rRNA and the mRNA was also proposed for translation initiation in eukaryotes. Here, we used an antisense RNA approach in vivo to identify the regions of 18S rRNA that might interact with the mRNA 5' untranslated region (5' UTR). Various fragments covering the entire mouse 18S rRNA gene were cloned 5' of a cat reporter gene in a eukaryotic vector, and translation products were analyzed after transient expression in human cells. For the largest part of 18S rRNA, we show that the insertion of complementary fragments in the mRNA 5' UTR do not impair translation of the downstream open reading frame (ORF). When translation inhibition is observed, reduction of the size of the complementary sequence to less than 200 nt alleviates the inhibitory effect. A single fragment complementary to the 18S rRNA 3' domain retains its inhibitory potential when reduced to 100 nt. Deletion analyses show that two distinct sequences of approximately 25 nt separated by a spacer sequence of 50 nt are required for the inhibitory effect. Sucrose gradient fractionation of polysomes reveals that mRNAs containing the inhibitory sequences accumulate in the fractions with 40S ribosomal subunits, suggesting that translation is blocked due to stalling of initiation complexes. Our results support an mRNA-rRNA base pairing to explain the translation inhibition observed and suggest that this region of 18S rRNA is properly located for interacting with mRNA.
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