ArticleNucleic acids research2018
The ribosomal A-site finger is crucial for binding and activation of the stringent factor RelA.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 56 citations in OpenAlex.
- The (p)ppGpp Synthetase RelA Contributes to Virulence, Competition Capability and Antibiotic Resistance of Avian PathogenicMicroorganisms · 2026Article
- Structural Basis of pppGpp Binding to the N-Terminal Domain of the Bifunctional RelA/SpoT Homolog RelInternational journal of molecular sciences · 2026Article
- Nanobody-mediated control of long RSH Rel and RelA catalysis by restriction of their conformational landscape.Nature communications · 2026Article
- Controlled Delivery and Light-Induced Release of Magic Spot Nucleotides in Escherichia coli.Angewandte Chemie (International ed. in English) · 2026Article
- Dissection of amino acid acquisition pathways demonstrates that amino acid starvation of Borrelia burgdorferi results in a (p)ppGpp-independent maladaptive response.Communications biology · 2025Article
- Starvation sensing by mycobacterial RelA/SpoT homologue through constitutive surveillance of translation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Sound the (Smaller) Alarm: The Triphosphate Magic Spot Nucleotide pGpp.Infection and immunity · 2023Review
- Sarecycline inhibits protein translation in Cutibacterium acnes 70S ribosome using a two-site mechanism.Nucleic acids research · 2023Article
- Thiostrepton, a resurging drug inhibiting the stringent response to counteract antibiotic-resistance and expression of virulence determinants inFrontiers in microbiology · 2023Article
- Fusion of the N-terminal 119 amino acids of RelA with the CTD domain render growth inhibitory effects of the latter, (p)ppGpp-dependent.Molecular genetics and genomics : MGG · 2022Article
- Awakening sleeper cells: a narrative review on bacterial magic spot synthetases as potential drug targets to overcome persistence.Current genetics · 2022Review
- Regulatory Themes and Variations by the Stress-Signaling Nucleotide Alarmones (p)ppGpp in Bacteria.Annual review of genetics · 2021Review
- The stringent response and physiological roles of (pp)pGpp in bacteria.Nature reviews. Microbiology · 2021Review
- The RelA hydrolase domain acts as a molecular switch for (p)ppGpp synthesis.Communications biology · 2021Article
- Ribosome association primes the stringent factor Rel for tRNA-dependent locking in the A-site and activation of (p)ppGpp synthesis.Nucleic acids research · 2021Article
- Four Phosphates at One Blow: Access to Pentaphosphorylated Magic Spot Nucleotides and Their Analysis by Capillary Electrophoresis.The Journal of organic chemistry · 2020Article
- A nucleotide-switch mechanism mediates opposing catalytic activities of Rel enzymes.Nature chemical biology · 2020Article
- Possible Roles for Basal Levels of (p)ppGpp: Growth Efficiency Vs. Surviving Stress.Frontiers in microbiology · 2020Review
- Functional Insights Into the Role ofFrontiers in microbiology · 2020Article
- The C-Terminal RRM/ACT Domain Is Crucial for Fine-Tuning the Activation of 'Long' RelA-SpoT Homolog Enzymes by Ribosomal Complexes.Frontiers in microbiology · 2020Article
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Authors and funding
12 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During amino acid starvation the Escherichia coli stringent response factor RelA recognizes deacylated tRNA in the ribosomal A-site. This interaction activates RelA-mediated synthesis of alarmone nucleotides pppGpp and ppGpp, collectively referred to as (p)ppGpp. These two alarmones are synthesized by addition of a pyrophosphate moiety to the 3' position of the abundant cellular nucleotide GTP and less abundant nucleotide GDP, respectively. Using untagged native RelA we show that allosteric activation of RelA by pppGpp increases the efficiency of GDP conversion to achieve the maximum rate of (p)ppGpp production. Using a panel of ribosomal RNA mutants, we show that the A-site finger structural element of 23S rRNA helix 38 is crucial for RelA binding to the ribosome and consequent activation, and deletion of the element severely compromises (p)ppGpp accumulation in E. coli upon amino acid starvation. Through binding assays and enzymology, we show that E. coli RelA does not form a stable complex with, and is not activated by, deacylated tRNA off the ribosome. This indicates that in the cell, RelA first binds the empty A-site and then recruits tRNA rather than first binding tRNA and then binding the ribosome.
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