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. 2021 Feb 11;11:3592. doi: 10.1038/s41598-021-82950-6

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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The AtYefM antitoxin blocks AtYoeB-mediated DNA cleavage, but it readily undergoes degradation that releases AtYoeB catalytic activity. (a) DNA degradation is not present for 10 µM co-purified AtYoeB-YefM complex immediately after purification. (b) After incubation for 1 week at temperatures above 4 °C, however, DNA cleavage activity is apparent. (c) Electrophoretic analysis of the protein samples used in panel (b) reveals degradation of one of the protein components that increases after storage at 23 °C and 37 °C (relative to 4 °C). Resolution of the doublet for intact AtYefM antitoxin requires a high percentage (18%) tris-tricine acrylamide gel. (d) Western blots were used to identify the individual bands visualized in the gel in panel (c), revealing that the degraded component is the His-tagged AtYefM antitoxin, while the Strep-tagged AtYoeB toxin remains unchanged. Note that the lowest band that accumulates is likely degraded AtYefM antitoxin, which appears to no longer carry the N-terminal His tag. (Full images of blots are provided in Fig. S6).