ArticleMicrobiologyOpen2015
YoeB toxin is activated during thermal stress.
Article in MicrobiologyOpen, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 32 citations in OpenAlex.
- Integrative Genomic and Structural Analysis Reveals Diversity and Stability of yefM-yoeBCurrent microbiology · 2026Article
- Contribution of Toxin-Antitoxin Systems to Adherent-InvasiveMicroorganisms · 2024Review
- Toxin-antitoxin genes are differentially expressed inFrontiers in microbiology · 2024Article
- Expression of type II toxin-antitoxin systems and ClpP protease of methicillin-resistantIranian journal of microbiology · 2021Article
- A YoeB toxin cleaves both RNA and DNA.Scientific reports · 2021Article
- Article
- Stress Can Induce Transcription of Toxin-Antitoxin Systems without Activating Toxin.Molecular cell · 2020Article
- Review
- Type II Toxin-Antitoxin Systems: Evolution and Revolutions.Journal of bacteriology · 2020Review
- Identifying a Molecular Mechanism That Imparts Species-Specific Toxicity to YoeB Toxins.Frontiers in microbiology · 2020Article
- Monomeric YoeB toxin retains RNase activity but adopts an obligate dimeric form for thermal stability.Nucleic acids research · 2019Article
- Article
- The toxin from a ParDE toxin-antitoxin system found in Pseudomonas aeruginosa offers protection to cells challenged with anti-gyrase antibiotics.Molecular microbiology · 2019Article
- Toxins targeting transfer RNAs: Translation inhibition by bacterial toxin-antitoxin systems.Wiley interdisciplinary reviews. RNA · 2019Review
- Functional insights into the Streptococcus pneumoniae HicBA toxin-antitoxin system based on a structural study.Nucleic acids research · 2018Article
- Complete genome sequence ofStandards in genomic sciences · 2018Article
- Functional details of the Mycobacterium tuberculosis VapBC26 toxin-antitoxin system based on a structural study: insights into unique binding and antibiotic peptides.Nucleic acids research · 2017Article
- mRNA bound to the 30S subunit is a HigB toxin substrate.RNA (New York, N.Y.) · 2016Article
- Review
- Wake me when it's over - Bacterial toxin-antitoxin proteins and induced dormancy.Experimental biology and medicine (Maywood, N.J.) · 2016Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Type II toxin-antitoxin (TA) modules are thought to mediate stress-responses by temporarily suppressing protein synthesis while cells redirect transcription to adapt to environmental change. Here, we show that YoeB, a ribosome-dependent mRNase toxin, is activated in Escherichia coli cells grown at elevated temperatures. YoeB activation is dependent on Lon protease, suggesting that thermal stress promotes increased degradation of the YefM antitoxin. Though YefM is efficiently degraded in response to Lon overproduction, we find that Lon antigen levels do not increase during heat shock, indicating that another mechanism accounts for temperature-induced YefM proteolysis. These observations suggest that YefM/YoeB functions in adaptation to temperature stress. However, this response is distinct from previously described models of TA function. First, YoeB mRNase activity is maintained over several hours of culture at 42°C, indicating that thermal activation is not transient. Moreover, heat-activated YoeB does not induce growth arrest nor does it suppress global protein synthesis. In fact, E. coli cells proliferate more rapidly at elevated temperatures and instantaneously accelerate their growth rate in response to acute heat shock. We propose that heat-activated YoeB may serve a quality control function, facilitating the recycling of stalled translation complexes through ribosome rescue pathways.
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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.