ArticleJournal of bacteriology2008
Conserved residues Asp16 and Pro24 of TnaC-tRNAPro participate in tryptophan induction of Tna operon expression.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 46 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
- Dynamics of transcription-translation coordination tune bacterial indole signaling.Nature chemical biology · 2020Article
- Regulation of Bacterial Gene Expression by Transcription Attenuation.Microbiology and molecular biology reviews : MMBR · 2019Review
- High-throughput in vivo mapping of RNA accessible interfaces to identify functional sRNA binding sites.Nature communications · 2018Article
- The cytochrome bd oxidase of Escherichia coli prevents respiratory inhibition by endogenous and exogenous hydrogen sulfide.Molecular microbiology · 2016Article
- Regulation of bacterial gene expression by ribosome stalling and rescuing.Current genetics · 2016Review
- Nascent chain-monitored remodeling of the Sec machinery for salinity adaptation of marine bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The ribosome can discriminate the chirality of amino acids within its peptidyl-transferase center.Proceedings of the National Academy of Sciences of the United States of America · 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
- Crucial elements that maintain the interactions between the regulatory TnaC peptide and the ribosome exit tunnel responsible for Trp inhibition of ribosome function.Nucleic acids research · 2012Article
- Birth, life and death of nascent polypeptide chains.Biotechnology journal · 2011Review
- S-adenosyl-L-methionine induces compaction of nascent peptide chain inside the ribosomal exit tunnel upon translation arrest in the Arabidopsis CGS1 gene.The Journal of biological chemistry · 2011Article
- Two groups of phenylalanine biosynthetic operon leader peptides genes: a high level of apparently incidental frameshifting in decoding Escherichia coli pheL.Nucleic acids research · 2011Article
- Isolation of translating ribosomes containing peptidyl-tRNAs for functional and structural analyses.Journal of visualized experiments : JoVE · 2011Article
- Sequence requirements for ribosome stalling by the arginine attenuator peptide.The Journal of biological chemistry · 2010Article
- Recognition of the regulatory nascent chain TnaC by the ribosome.Structure (London, England : 1993) · 2010Article
- Divergent stalling sequences sense and control cellular physiology.Biochemical and biophysical research communications · 2010Review
- Structural insight into nascent polypeptide chain-mediated translational stalling.Science (New York, N.Y.) · 2009Article
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2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Escherichia coli, interactions between the nascent TnaC-tRNA(Pro) peptidyl-tRNA and the translating ribosome create a tryptophan binding site in the ribosome where bound tryptophan inhibits TnaC-tRNA(Pro) cleavage. This inhibition delays ribosome release, thereby inhibiting Rho factor binding and action, resulting in increased tna operon transcription. Replacing Trp12 of TnaC with any other amino acid residue was previously shown to prevent tryptophan binding and induction of tna operon expression. Genome-wide comparisons of TnaC amino acid sequences identify Asp16 and Pro24, as well as Trp12, as highly conserved TnaC residues. Replacing these residues with other residues was previously shown to influence tryptophan induction of tna operon expression. In this study, in vitro analyses were performed to examine the potential roles of Asp16 and Pro24 in tna operon induction. Replacing Asp16 or Pro24 of TnaC of E. coli with other amino acids established that these residues are essential for free tryptophan binding and inhibition of TnaC-tRNA(Pro) cleavage at the peptidyl transferase center. Asp16 and Pro24 are in fact located in spatial positions corresponding to critical residues of AAP, another ribosome regulatory peptide. Sparsomycin-methylation protection studies further suggested that segments of 23S RNA were arranged differently in ribosomes bearing TnaCs with either the Asp16Ala or the Pro24Ala change. Thus, features of the amino acid sequence of TnaC of the nascent TnaC-tRNA(Pro) peptidyl-tRNA, in addition to the presence of Trp12, are necessary for the nascent peptide to create a tryptophan binding/inhibition site in the translating ribosome.
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