ClpAP protease is a universal factor that activates the parDE toxin-antitoxin system from a broad host range RK2 plasmid
| Autor: | Igor Konieczny, Andrzej Dubiel, Adam P. Kupinski, Katarzyna Wegrzyn |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Proteases Proteolysis medicine.medical_treatment Bacterial Toxins lcsh:Medicine medicine.disease_cause complex mixtures Article 03 medical and health sciences Plasmid Caulobacter crescentus Escherichia coli medicine RK2 plasmid lcsh:Science Multidisciplinary Protease medicine.diagnostic_test Pseudomonas putida Chemistry Escherichia coli Proteins lcsh:R Toxin-Antitoxin Systems DNA Endopeptidase Clp Toxin-antitoxin system Cell biology DNA-Binding Proteins 030104 developmental biology lcsh:Q Antitoxin Plasmids Protein Binding |
| Zdroj: | Scientific Reports Scientific Reports, Vol 8, Iss 1, Pp 1-12 (2018) |
| ISSN: | 2045-2322 |
| DOI: | 10.1038/s41598-018-33726-y |
| Popis: | The activity of type II toxin-antitoxin systems (TA), which are responsible for many important features of bacterial cells, is based on the differences between toxin and antitoxin stabilities. The antitoxin lability results from bacterial protease activity. Here, we investigated how particular Escherichia coli cytosolic proteases, namely, Lon, ClpAP, ClpXP, and ClpYQ, affect the stability of both the toxin and antitoxin components of the parDE system from the broad host range plasmid RK2. The results of our in vivo and in vitro experiments show that the ParD antitoxin is degraded by the ClpAP protease, and dsDNA stimulates this process. The ParE toxin is not degraded by any of these proteases and can therefore cause growth inhibition of plasmid-free cells after an unequal plasmid distribution during cell division. We also demonstrate that the ParE toxin interaction with ParD prevents antitoxin proteolysis by ClpAP; however, this interaction does not prevent the ClpAP interaction with ParD. We show that ClpAP protease homologs affect plasmid stability in other bacterial species, indicating that ClpAP is a universal activator of the parDE system and that ParD is a universal substrate for ClpAP. |
| Databáze: | OpenAIRE |
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