ArticleNucleic acids research2007
Structural elements defining elongation factor Tu mediated suppression of codon ambiguity.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 42 citations in OpenAlex.
- Role of factor H-related protein 3 inFrontiers in immunology · 2024Article
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- On the Track of the Missing tRNA Genes: A Source of Non-Canonical Functions?Frontiers in molecular biosciences · 2021Review
- Function and origin of mistranslation in distinct cellular contexts.Critical reviews in biochemistry and molecular biology · 2017Review
- Article
- The essential mycobacterial amidotransferase GatCAB is a modulator of specific translational fidelity.Nature microbiology · 2016Article
- Outwitting EF-Tu and the ribosome: translation with d-amino acids.Nucleic acids research · 2015Article
- Effect of hydrogen peroxide on the biosynthesis of heme and proteins: potential implications for the partitioning of Glu-tRNA(Glu) between these pathways.International journal of molecular sciences · 2014Article
- A tRNA body with high affinity for EF-Tu hastens ribosomal incorporation of unnatural amino acids.RNA (New York, N.Y.) · 2014Article
- tRNAs as regulators of biological processes.Frontiers in genetics · 2014Review
- Direction of aminoacylated transfer RNAs into antibiotic synthesis and peptidoglycan-mediated antibiotic resistance.FEBS letters · 2013Review
- Article
- A tRNA-independent mechanism for transamidosome assembly promotes aminoacyl-tRNA transamidation.The Journal of biological chemistry · 2013Article
- Riboswitch (T-box)-mediated control of tRNA-dependent amidation in Clostridium acetobutylicum rationalizes gene and pathway redundancy for asparagine and asparaginyl-trnaasn synthesis.The Journal of biological chemistry · 2012Article
- The asparagine-transamidosome from Helicobacter pylori: a dual-kinetic mode in non-discriminating aspartyl-tRNA synthetase safeguards the genetic code.Nucleic acids research · 2012Article
- Histidine 66 in Escherichia coli elongation factor tu selectively stabilizes aminoacyl-tRNAs.The Journal of biological chemistry · 2012Article
- Elongation factor 1β' gene from Spodoptera exigua: characterization and function identification through RNA interference.International journal of molecular sciences · 2012Article
- Is the sequence-specific binding of aminoacyl-tRNAs by EF-Tu universal among bacteria?Nucleic acids research · 2011Article
- Gln-tRNAGln synthesis in a dynamic transamidosome from Helicobacter pylori, where GluRS2 hydrolyzes excess Glu-tRNAGln.Nucleic acids research · 2011Article
- Characterization of Gtf1p, the connector subunit of yeast mitochondrial tRNA-dependent amidotransferase.The Journal of biological chemistry · 2011Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In most prokaryotes Asn-tRNA(Asn) and Gln-tRNA(Gln) are formed by amidation of aspartate and glutamate mischarged onto tRNA(Asn) and tRNA(Gln), respectively. Coexistence in the organism of mischarged Asp-tRNA(Asn) and Glu-tRNA(Gln) and the homologous Asn-tRNA(Asn) and Gln-tRNA(Gln) does not, however, lead to erroneous incorporation of Asp and Glu into proteins, since EF-Tu discriminates the misacylated tRNAs from the correctly charged ones. This property contrasts with the canonical function of EF-Tu, which is to non-specifically bind the homologous aa-tRNAs, as well as heterologous species formed in vitro by aminoacylation of non-cognate tRNAs. In Thermus thermophilus that forms the Asp-tRNA(Asn) intermediate by the indirect pathway of tRNA asparaginylation, EF-Tu must discriminate the mischarged aminoacyl-tRNAs (aa-tRNA). We show that two base pairs in the tRNA T-arm and a single residue in the amino acid binding pocket of EF-Tu promote discrimination of Asp-tRNA(Asn) from Asn-tRNA(Asn) and Asp-tRNA(Asp) by the protein. Our analysis suggests that these structural elements might also contribute to rejection of other mischarged aa-tRNAs formed in vivo that are not involved in peptide elongation. Additionally, these structural features might be involved in maintaining a delicate balance of weak and strong binding affinities between EF-Tu and the amino acid and tRNA moieties of other elongator aa-tRNAs.
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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.