What determines whether mammalian ribosomes resume scanning after translation of a short upstream open reading frame?
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Summary
Reinitiation in vitro suggests that resumption of scanning may depend on the interaction between eIF4F (or the eIF 4G central domain) and the ribosome being maintained while the Ribosome translates the sORF.
- Type
- article
- Published
- 2004-01-01
- Cited by
- 180
- References
- 44
- Access
- Open access
- OpenAlex
- https://openalex.org/W1976860224
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:29621143
Keywords
Biology, EIF4G, Upstream open reading frame, Open reading frame, Start codon
References
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- Translational control of gene expression
- The specificities of yeast methionine aminopeptidase and acetylation of amino-terminal methionine in vivo. Processing of altered iso-1-cytochromes c created by oligonucleotide transformation.
- Cotranslational amino-terminal processing of cytosolic proteins. Cell-free expression of site-directed mutants of human hemoglobin.
- Dominant negative mutants of mammalian translation initiation factor eIF‐4A define a critical role for eIF‐4F in cap‐dependent and cap‐independent initiation of translation.
- Ribosome pausing and stacking during translation of a eukaryotic mRNA.
- Modulation of tRNA(iMet), eIF-2, and eIF-2B expression shows that GCN4 translation is inversely coupled to the level of eIF-2.GTP.Met-tRNA(iMet) ternary complexes
- Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry
- Synthesis in vitro of a seven amino acid peptide encoded in the leader RNA of Rous sarcoma virus.
- Introduction of homologous DNA sequences into mammalian cells induces mutations in the cognate gene
- mRNA sequences influencing translation and the selection of AUG initiator codons in the yeast Saccharomyces cerevisiae
- Evidence that translation reinitiation abrogates nonsense‐mediated mRNA decay in mammalian cells
- Factorless ribosome assembly on the internal ribosome entry site of cricket paralysis virus.
- Initiation of protein synthesis: evidence for messenger RNA-independent binding of methionyl-transfer RNA to the 40 S ribosomal subunit.
- A reassessment of the translation initiation codon in vertebrates.
- An unusual coordinated cleavage event in the processing of encephalomyocarditis virus polypeptides.
- Initiation of translation of human rhinovirus RNA: mapping the internal ribosome entry site.
Cited by
- Regulation of Eukaryotic Translation Initiation by Signal Transduction
- Charting DENR-dependent translation reinitiation uncovers predictive uORF features and links to circadian timekeeping via Clock
- Termination and post-termination events in eukaryotic translation.
- miRNA Effects on mRNA closed-loop formation during translation initiation.
- Alternative Translation Strategies in Plant Viruses
- Chapter 3 Virus Versus Host Cell Translation
- The role of poly(A)-binding protein in microRNA-mediated repression
- Studies of recombinant protein expression : targeting signals, 3' untranslated regions and trans-acting factors
- Reinitiation at non-canonical start codons leads to leak expression when incorporating unnatural amino acids
- Chapter 9 Viral Strategies to Subvert the Mammalian Translation Machinery
- The regulatory potential of upstream open reading frames in eukaryotic gene expression
- The molecular basis of translational control.
- Translational Regulation of mRNAs encoding SAPAP3 in Rattus norvegicus
- Novel molecular pathologies in asthma and COPD
- Methods to analyze microRNA-mediated control of mRNA translation.
- Getting the message in protein synthesis
- Analysis of the canonical initiation and trans-acting factor requirements of 5'TOP containing mRNAs
- Investigating Translational Reprogramming In Cellular Stress Response By Elongation Pausing And Alternative Initiation
- Visualising ribosome profiling and using it for reading frame detection and exploration of eukaryotic translation initiation
- Multiple elements in the eIF4G1 N‐terminus promote assembly of eIF4G1•PABP mRNPs in vivo
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