ArticleNature chemical biology2013
The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu.
Article in Nature chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.
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Who cites it
108 citing papers in PubMed, 171 citations in OpenAlex.
- Article
- Toxin dimerization and a distinct DNA-binding architecture define chromosomal Phd-Doc regulation.Nucleic acids research · 2026Article
- Protein-Protein Interactions as Promising Molecular Targets for Novel Antimicrobials Aimed at Gram-Negative Bacteria.International journal of molecular sciences · 2025Review
- A Programmable Finite-Replicated Organism Framework for Balanced Safety and Functionality.Life (Basel, Switzerland) · 2025Article
- Article
- A single vector system for tunable and homogeneous dual gene expression in Escherichia coli.Scientific reports · 2025Article
- Article
- Dynamic Protein Phosphorylation inMicroorganisms · 2024Article
- Single-cell evidence for plasmid addiction mediated by toxin-antitoxin systems.Nucleic acids research · 2024Article
- TheApplied and environmental microbiology · 2024Article
- Article
- Friend or Foe: Protein Inhibitors of DNA Gyrase.Biology · 2024Review
- Unraveling the evolutionary dynamics of toxin-antitoxin systems in diverse genetic lineages ofmBio · 2024Article
- Stapled Phd Peptides Inhibit Doc Toxin Induced Growth Arrest inACS chemical biology · 2023Article
- Type II bacterial toxin-antitoxins: hypotheses, facts, and the newfound plethora of the PezAT system.FEMS microbiology reviews · 2023Article
- The structural basis of hyperpromiscuity in a core combinatorial network of type II toxin-antitoxin and related phage defense systems.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Applications of toxin-antitoxin systems in synthetic biology.Engineering microbiology · 2023Review
- Toxin-antitoxin systems in bacterial pathogenesis.Heliyon · 2023Review
- AMPylation of small GTPases by Fic enzymes.FEBS letters · 2023Review
- The DarT/DarG Toxin-Antitoxin ADP-Ribosylation System as a Novel Target for a Rational Design of Innovative Antimicrobial Strategies.Pathogens (Basel, Switzerland) · 2023Article
48 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Fic proteins are ubiquitous in all of the domains of life and have critical roles in multiple cellular processes through AMPylation of (transfer of AMP to) target proteins. Doc from the doc-phd toxin-antitoxin module is a member of the Fic family and inhibits bacterial translation by an unknown mechanism. Here we show that, in contrast to having AMPylating activity, Doc is a new type of kinase that inhibits bacterial translation by phosphorylating the conserved threonine (Thr382) of the translation elongation factor EF-Tu, rendering EF-Tu unable to bind aminoacylated tRNAs. We provide evidence that EF-Tu phosphorylation diverged from AMPylation by antiparallel binding of the NTP relative to the catalytic residues of the conserved Fic catalytic core of Doc. The results bring insights into the mechanism and role of phosphorylation of EF-Tu in bacterial physiology as well as represent an example of the catalytic plasticity of enzymes and a mechanism for the evolution of new enzymatic activities.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.