A YoeB toxin cleaves both RNA and DNA
Abstract Type II toxin-antitoxin systems contain a toxin protein, which mediates diverse interactions within the bacterial cell when it is not bound by its cognate antitoxin protein. These toxins provide a rich source of evolutionarily-conserved tertiary folds that mediate diverse catalytic reaction...
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Nature Portfolio
2021
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oai:doaj.org-article:733b37a7942248448dfa03ba464060162021-12-02T12:09:32ZA YoeB toxin cleaves both RNA and DNA10.1038/s41598-021-82950-62045-2322https://doaj.org/article/733b37a7942248448dfa03ba464060162021-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-82950-6https://doaj.org/toc/2045-2322Abstract Type II toxin-antitoxin systems contain a toxin protein, which mediates diverse interactions within the bacterial cell when it is not bound by its cognate antitoxin protein. These toxins provide a rich source of evolutionarily-conserved tertiary folds that mediate diverse catalytic reactions. These properties make toxins of interest in biotechnology applications, and studies of the catalytic mechanisms continue to provide surprises. In the current work, our studies on a YoeB family toxin from Agrobacterium tumefaciens have revealed a conserved ribosome-independent non-specific nuclease activity. We have quantified the RNA and DNA cleavage activity, revealing they have essentially equivalent dose-dependence while differing in requirements for divalent cations and pH sensitivity. The DNA cleavage activity is as a nickase for any topology of double-stranded DNA, as well as cleaving single-stranded DNA. AtYoeB is able to bind to double-stranded DNA with mid-micromolar affinity. Comparison of the ribosome-dependent and -independent reactions demonstrates an approximate tenfold efficiency imparted by the ribosome. This demonstrates YoeB toxins can act as non-specific nucleases, cleaving both RNA and DNA, in the absence of being bound within the ribosome.Julia McGillickJessica R. AmesTamiko MurphyChristina R. BourneNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-9 (2021) |
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Medicine R Science Q Julia McGillick Jessica R. Ames Tamiko Murphy Christina R. Bourne A YoeB toxin cleaves both RNA and DNA |
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Abstract Type II toxin-antitoxin systems contain a toxin protein, which mediates diverse interactions within the bacterial cell when it is not bound by its cognate antitoxin protein. These toxins provide a rich source of evolutionarily-conserved tertiary folds that mediate diverse catalytic reactions. These properties make toxins of interest in biotechnology applications, and studies of the catalytic mechanisms continue to provide surprises. In the current work, our studies on a YoeB family toxin from Agrobacterium tumefaciens have revealed a conserved ribosome-independent non-specific nuclease activity. We have quantified the RNA and DNA cleavage activity, revealing they have essentially equivalent dose-dependence while differing in requirements for divalent cations and pH sensitivity. The DNA cleavage activity is as a nickase for any topology of double-stranded DNA, as well as cleaving single-stranded DNA. AtYoeB is able to bind to double-stranded DNA with mid-micromolar affinity. Comparison of the ribosome-dependent and -independent reactions demonstrates an approximate tenfold efficiency imparted by the ribosome. This demonstrates YoeB toxins can act as non-specific nucleases, cleaving both RNA and DNA, in the absence of being bound within the ribosome. |
format |
article |
author |
Julia McGillick Jessica R. Ames Tamiko Murphy Christina R. Bourne |
author_facet |
Julia McGillick Jessica R. Ames Tamiko Murphy Christina R. Bourne |
author_sort |
Julia McGillick |
title |
A YoeB toxin cleaves both RNA and DNA |
title_short |
A YoeB toxin cleaves both RNA and DNA |
title_full |
A YoeB toxin cleaves both RNA and DNA |
title_fullStr |
A YoeB toxin cleaves both RNA and DNA |
title_full_unstemmed |
A YoeB toxin cleaves both RNA and DNA |
title_sort |
yoeb toxin cleaves both rna and dna |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/733b37a7942248448dfa03ba46406016 |
work_keys_str_mv |
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