Journal
NATURE CHEMICAL BIOLOGY
Volume 8, Issue 10, Pages 855-861Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.1062
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Funding
- US National Institutes of Health [R01 GM089999]
- US National Science Foundation (CAREER award) [MCB 0952550]
- 1000-Youth Elite Program from China.
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0952550] Funding Source: National Science Foundation
- Office of Integrative Activities
- Office Of The Director [1004057] Funding Source: National Science Foundation
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Among bacterial toxin-antitoxin systems, to date no antitoxin has been identified that functions by cleaving toxin mRNA. Here we show that YjdO (renamed GhoT) is a membrane lytic peptide that causes ghost cell formation (lysed cells with damaged membranes) and increases persistence (persister cells are tolerant to antibiotics without undergoing genetic change). GhoT is part of a new toxin-antitoxin system with YjdK (renamed GhoS) because in vitro RNA degradation studies, quantitative real-time reverse-transcription PCR and whole-transcriptome studies revealed that GhoS masks GhoT toxicity by cleaving specifically yjdO (ghoT) mRNA. Alanine substitutions showed that Arg28 is important for GhoS activity, and RNA sequencing indicated that the GhoS cleavage site is rich in U and A. The NMR structure of GhoS indicates it is related to the CRISPR-associated-2 RNase, and GhoS is a monomer. Hence, GhoT-GhoS is to our knowledge the first type V toxin-antitoxin system where a protein antitoxin inhibits the toxin by cleaving specifically its mRNA.
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