ArticleNucleic acids research2012
Crucial elements that maintain the interactions between the regulatory TnaC peptide and the ribosome exit tunnel responsible for Trp inhibition of ribosome function.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Structural basis of l-tryptophan-dependent inhibition of release factor 2 by the TnaC arrest peptide.Nucleic acids research · 2021Article
- Structural basis for the tryptophan sensitivity of TnaC-mediated ribosome stalling.Nature communications · 2021Article
- Conserved Upstream Open Reading Frame Nascent Peptides That Control Translation.Annual review of genetics · 2020Review
- A long-distance rRNA base pair impacts the ability of macrolide antibiotics to kill bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- mRNA regions where 80S ribosomes pause during translation elongation in vivo interact with protein uS19, a component of the decoding site.Nucleic acids research · 2020Article
- The regulatory TnaC nascent peptide preferentially inhibits release factor 2-mediated hydrolysis of peptidyl-tRNA.The Journal of biological chemistry · 2019Article
- Identification of Arabidopsis thaliana upstream open reading frames encoding peptide sequences that cause ribosomal arrest.Nucleic acids research · 2017Article
- High-resolution structure of the Escherichia coli ribosome.Nature structural & molecular biology · 2015Article
- Identification of novel Arabidopsis thaliana upstream open reading frames that control expression of the main coding sequences in a peptide sequence-dependent manner.Nucleic acids research · 2015Article
- Interactions of the TnaC nascent peptide with rRNA in the exit tunnel enable the ribosome to respond to free tryptophan.Nucleic acids research · 2014Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Translation of the TnaC nascent peptide inhibits ribosomal activity in the presence of l-tryptophan, inducing expression of the tnaCAB operon in Escherichia coli. Using chemical methylation, this work reveals how interactions between TnaC and the ribosome are affected by mutations in both molecules. The presence of the TnaC-tRNA(Pro) peptidyl-tRNA within the ribosome protects the 23S rRNA nucleotide U2609 against chemical methylation. Such protection was not observed in mutant ribosomes containing changes in 23S rRNA nucleotides of the A748-A752 region. Nucleotides A752 and U2609 establish a base-pair interaction. Most replacements of either A752 or U2609 affected Trp induction of a TnaC-regulated LacZ reporter. However, the single change A752G, or the dual replacements A752G and U2609C, maintained Trp induction. Replacements at the conserved TnaC residues W12 and D16 also abolished the protection of U2609 by TnaC-tRNA(Pro) against chemical methylation. These data indicate that the TnaC nascent peptide in the ribosome exit tunnel interacts with the U2609 nucleotide when the ribosome is Trp responsive. This interaction is affected by mutational changes in exit tunnel nucleotides of 23S rRNA, as well as in conserved TnaC residues, suggesting that they affect the structure of the exit tunnel and/or the nascent peptide configuration in the tunnel.
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