ArticleProceedings of the National Academy of Sciences of the United States of America2001
The mechanism of tryptophan induction of tryptophanase operon expression: tryptophan inhibits release factor-mediated cleavage of TnaC-peptidyl-tRNA(Pro).
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 125 citations in OpenAlex.
- Mechanism of ribosome stalling by the AMD1 C-terminal tail arrest peptide.Science advances · 2026Article
- pH regulates gut bacterial tryptophan metabolism.NPJ biofilms and microbiomes · 2026Article
- A montmorillonite-based oral fermentation system enables long-lasting in-situ biosynthesis to restore intestinal homeostasis.Nature communications · 2026Article
- Rho-dependent transcription termination: mechanisms and roles in bacterial fitness and adaptation to environmental changes.RNA (New York, N.Y.) · 2025Review
- Structure and dynamics of Proteus vulgaris tryptophan indole-lyase complexes with l-ethionine and l-alanine.Archives of biochemistry and biophysics · 2025Article
- Structural Snapshots ofACS catalysis · 2024Article
- Control of mRNA fate by its encoded nascent polypeptide.Molecular cell · 2023Review
- A method to enrich polypeptidyl-tRNAs to capture snapshots of translation in the cell.Nucleic acids research · 2023Article
- The Identity of the Constriction Region of the Ribosomal Exit Tunnel Is Important to Maintain Gene Expression in Escherichia coli.Microbiology spectrum · 2022Article
- Drop-off-reinitiation triggered by EF-G-driven mistranslocation and its alleviation by EF-P.Nucleic acids research · 2022Article
- The landscape of translational stall sites in bacteria revealed by monosome and disome profiling.RNA (New York, N.Y.) · 2022Article
- Structural basis of l-tryptophan-dependent inhibition of release factor 2 by the TnaC arrest peptide.Nucleic acids research · 2021Article
- A nascent polypeptide sequence modulates DnaA translation elongation in response to nutrient availability.eLife · 2021Article
- Structural basis for the tryptophan sensitivity of TnaC-mediated ribosome stalling.Nature communications · 2021Article
- Article
- Production of Tyrian purple indigoid dye from tryptophan in Escherichia coli.Nature chemical biology · 2021Article
- Dynamics of transcription-translation coordination tune bacterial indole signaling.Nature chemical biology · 2020Article
- An Upstream Open Reading Frame Represses Translation of Chicken PPARγ Transcript Variant 1.Frontiers in genetics · 2020Article
- The regulatory TnaC nascent peptide preferentially inhibits release factor 2-mediated hydrolysis of peptidyl-tRNA.The Journal of biological chemistry · 2019Article
- CRISPR/Cas9-facilitated engineering with growth-coupled and sensor-guidedMetabolic engineering communications · 2019Article
3 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Expression of the tryptophanase (tna) operon of Escherichia coli is regulated by catabolite repression and tryptophan-induced transcription antitermination. In a previous study, we reproduced the regulatory features of this operon observed in vivo by using an in vitro S-30 system. We also found that, under inducing conditions, the leader peptidyl-tRNA (TnaC-peptidyl-tRNA(Pro)) is not cleaved; it accumulates in the S-30 reaction mixture. In this paper, we examine the requirements for TnaC-peptidyl-tRNA(Pro) accumulation and cleavage, in vitro. We show that this peptidyl-tRNA remains bound to the translating ribosome. Removal of free tryptophan and addition of release factor 1 or 2 leads to hydrolysis of TnaC-peptidyl-tRNA(Pro) and release of TnaC from the ribosome-mRNA complex. Release factor-mediated cleavage is prevented by the addition of tryptophan. TnaC of the ribosome-bound TnaC-peptidyl-tRNA(Pro) was transferable to puromycin. This transfer was also blocked by tryptophan. Tests with various tryptophan analogs as substitutes for tryptophan revealed the existence of strict structural requirements for tryptophan action. Our findings demonstrate that the addition of tryptophan to ribosomes bearing nascent TnaC-peptidyl-tRNA(Pro) inhibits both TnaC peptidyl-tRNA(Pro) hydrolysis and TnaC peptidyl transfer. The associated translating ribosome therefore remains attached to the leader transcript where it blocks Rho factor binding and subsequent transcription termination.
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