ArticleThe Journal of biological chemistry2013
Elongation factor Ts directly facilitates the formation and disassembly of the Escherichia coli elongation factor Tu·GTP·aminoacyl-tRNA ternary complex.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 44 citations in OpenAlex.
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- 16S rRNA methyltransferase KsgA contributes to oxidative stress and antibiotic resistance in Pseudomonas aeruginosa.Scientific reports · 2024Article
- β-Amino Acids Reduce Ternary Complex Stability and Alter the Translation Elongation Mechanism.ACS central science · 2024Article
- β-amino acids reduce ternary complex stability and alter the translation elongation mechanism.bioRxiv : the preprint server for biology · 2024Article
- Tuning tRNAs for improved translation.Frontiers in genetics · 2024Review
- Polyclonal antibodies inhibit growth of key cellulolytic rumen bacterial species.Frontiers in microbiology · 2023Article
- Elongation factor P modulatesProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Microbial Proteins in Stomach Biopsies Associated with Gastritis, Ulcer, and Gastric Cancer.Molecules (Basel, Switzerland) · 2022Article
- Mechanistic insights into tRNA cleavage by a contact-dependent growth inhibitor protein and translation factors.Nucleic acids research · 2022Article
- Mutational analysis reveals potential phosphorylation sites in eukaryotic elongation factor 1A that are important for its activity.FEBS letters · 2021Article
- Transposon Insertion in thePathogens (Basel, Switzerland) · 2020Article
- Elongation factor-Tu can repetitively engage aminoacyl-tRNA within the ribosome during the proofreading stage of tRNA selection.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A novel TUFM homozygous variant in a child with mitochondrial cardiomyopathy expands the phenotype of combined oxidative phosphorylation deficiency 4.Journal of human genetics · 2019Article
- A 2D-DIGE-based proteomic analysis brings new insights into cellular responses of Pseudomonas putida KT2440 during polyhydroxyalkanoates synthesis.Microbial cell factories · 2019Article
- Understanding the high L-valine production in Corynebacterium glutamicum VWB-1 using transcriptomics and proteomics.Scientific reports · 2018Article
- Article
- Miscoding-induced stalling of substrate translocation on the bacterial ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structure of a novel antibacterial toxin that exploits elongation factor Tu to cleave specific transfer RNAs.Nucleic acids research · 2017Article
- Fail-safe control of translation initiation by dissociation of eIF2α phosphorylated ternary complexes.eLife · 2017Article
- Activation of contact-dependent antibacterial tRNase toxins by translation elongation factors.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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7 authors at 1 institution in 1 country.
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Abstract
backgroundAminoacyl-tRNA (aa-tRNA) enters the ribosome in a ternary complex with the G-protein elongation factor Tu (EF-Tu) and GTP.
resultsEF-Tu·GTP·aa-tRNA ternary complex formation and decay rates are accelerated in the presence of the nucleotide exchange factor elongation factor Ts (EF-Ts).
conclusionEF-Ts directly facilitates the formation and disassociation of ternary complex. SIGNIFICANCE: This system demonstrates a novel function of EF-Ts. Aminoacyl-tRNA enters the translating ribosome in a ternary complex with elongation factor Tu (EF-Tu) and GTP. Here, we describe bulk steady state and pre-steady state fluorescence methods that enabled us to quantitatively explore the kinetic features of Escherichia coli ternary complex formation and decay. The data obtained suggest that both processes are controlled by a nucleotide-dependent, rate-determining conformational change in EF-Tu. Unexpectedly, we found that this conformational change is accelerated by elongation factor Ts (EF-Ts), the guanosine nucleotide exchange factor for EF-Tu. Notably, EF-Ts attenuates the affinity of EF-Tu for GTP and destabilizes ternary complex in the presence of non-hydrolyzable GTP analogs. These results suggest that EF-Ts serves an unanticipated role in the cell of actively regulating the abundance and stability of ternary complex in a manner that contributes to rapid and faithful protein synthesis.
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