ClpAP protease is a universal factor that activates the parDE toxin-antitoxin system from a broad host range RK2 plasmid

Andrzej Dubiel , Katarzyna Węgrzyn , Adam Kupiński , Igor Konieczny

Abstract

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.
Author Andrzej Dubiel (IFB / ZLS)
Andrzej Dubiel,,
- Zespół Laboratoriów Specjalistycznych MWB UG i GUMed
, Katarzyna Węgrzyn (IFB / M020 / DMCB)
Katarzyna Węgrzyn,,
- Department of Molecular and Cellular Biology
, Adam Kupiński (IFB)
Adam Kupiński,,
- Intercollegiate Faculty of Biotechnology UG
, Igor Konieczny (IFB / M020 / DMCB)
Igor Konieczny,,
- Department of Molecular and Cellular Biology
Journal seriesScientific Reports, ISSN 2045-2322, (A 40 pkt)
Issue year2018
Vol8
Pages1-12
Publication size in sheets0.55
Article number15287
ASJC Classification1000 Multidisciplinary
DOIDOI:10.1038/s41598-018-33726-y
URL https://www.nature.com/articles/s41598-018-33726-y
Languageen angielski
LicenseJournal (articles only); published final; Uznanie Autorstwa (CC-BY); with publication
Score (nominal)40
Score sourcejournalList
ScoreMinisterial score = 40.0, 03-02-2020, ArticleFromJournal
Publication indicators Scopus SNIP (Source Normalised Impact per Paper): 2016 = 1.401; WoS Impact Factor: 2018 = 4.011 (2) - 2018=4.525 (5)
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