ArticleNucleic acids research2013
YoeB-ribosome structure: a canonical RNase that requires the ribosome for its specific activity.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 57 citations in OpenAlex.
- Phenotypic and Genomic Divergence in Biofilm Formation in STEC and Non-STECPathogens (Basel, Switzerland) · 2026Article
- The HigB-like SehA toxin promotes non-replicating Salmonella inside macrophages by inhibiting ribonuclease III-dependent rRNA maturation.Nucleic acids research · 2026Article
- Carrot and stick: how RNase R contributes to function and destruction of the translation machinery.RNA biology · 2025Review
- Ribonuclease toxin RelE1 inhibits growth of Mycobacterium tuberculosis through specific cleavage of the ribosomal anti-Shine-Dalgarno region.Nucleic acids research · 2025Article
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- Type II Toxin-Antitoxin Systems inInfection and drug resistance · 2025Review
- Substrate recognition and cryo-EM structure of the ribosome-bound TAC toxin of Mycobacterium tuberculosis.Nature communications · 2022Article
- Article
- Genome Sequencing of fiveMicroorganisms · 2021Article
- A YoeB toxin cleaves both RNA and DNA.Scientific reports · 2021Article
- Substrate specificity of bacterial endoribonuclease toxins.BMB reports · 2020Review
- Distinct oligomeric structures of the YoeB-YefM complex provide insights into the conditional cooperativity of type II toxin-antitoxin system.Nucleic acids research · 2020Article
- The Positively Charged Active Site of the Bacterial Toxin RelE Causes a Large Shift in the General Base pBiochemistry · 2020Article
- Identifying a Molecular Mechanism That Imparts Species-Specific Toxicity to YoeB Toxins.Frontiers in microbiology · 2020Article
- The Variety in the Common Theme of Translation Inhibition by Type II Toxin-Antitoxin Systems.Frontiers in genetics · 2020Review
- Monomeric YoeB toxin retains RNase activity but adopts an obligate dimeric form for thermal stability.Nucleic acids research · 2019Article
- Identification and first characterization of DinJ-YafQ toxin-antitoxin systems in Lactobacillus species of biotechnological interest.Scientific reports · 2019Article
- Structure of a novel antibacterial toxin that exploits elongation factor Tu to cleave specific transfer RNAs.Nucleic acids research · 2017Article
- Death by translation: ribosome-assisted degradation of mRNA by endonuclease toxins.FEBS letters · 2017Article
- Ribosome-dependent Vibrio cholerae mRNAse HigB2 is regulated by a β-strand sliding mechanism.Nucleic acids research · 2017Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As a typical endoribonuclease, YoeB mediates cellular adaptation in diverse bacteria by degrading mRNAs on its activation. Although the catalytic core of YoeB is thought to be identical to well-studied nucleases, this enzyme specifically targets mRNA substrates that are associated with ribosomes in vivo. However, the molecular mechanism of mRNA recognition and cleavage by YoeB, and the requirement of ribosome for its optimal activity, largely remain elusive. Here, we report the structure of YoeB bound to 70S ribosome in pre-cleavage state, revealing that both the 30S and 50S subunits participate in YoeB binding. The mRNA is recognized by the catalytic core of YoeB, of which the general base/acid (Glu46/His83) are within hydrogen-bonding distance to their reaction atoms, demonstrating an active conformation of YoeB on ribosome. Also, the mRNA orientation involves the universally conserved A1493 and G530 of 16S rRNA. In addition, mass spectrometry data indicated that YoeB cleaves mRNA following the second position at the A-site codon, resulting in a final product with a 3'-phosphate at the newly formed 3' end. Our results demonstrate a classical acid-base catalysis for YoeB-mediated RNA hydrolysis and provide insight into how the ribosome is essential for its specific activity.
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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.