Author
Listed:
- Michal Bukowski
(Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Krakow, Poland)
- Robert Lyzen
(University of Gdansk, Wita Stwosza 59, 80-308 Gdansk, Poland)
- Weronika M. Helbin
(Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Krakow, Poland)
- Emilia Bonar
(Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Krakow, Poland)
- Agnieszka Szalewska-Palasz
(University of Gdansk, Wita Stwosza 59, 80-308 Gdansk, Poland)
- Grzegorz Wegrzyn
(University of Gdansk, Wita Stwosza 59, 80-308 Gdansk, Poland)
- Grzegorz Dubin
(Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Krakow, Poland
Malopolska Centre of Biotechnology, Gronostajowa 7, 30-387 Krakow, Poland)
- Adam Dubin
(Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Krakow, Poland)
- Benedykt Wladyka
(Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Krakow, Poland
Malopolska Centre of Biotechnology, Gronostajowa 7, 30-387 Krakow, Poland)
Abstract
Toxin–antitoxin systems were shown to be involved in plasmid maintenance when they were initially discovered, but other roles have been demonstrated since. Here we identify and characterize a novel toxin–antitoxin system (pemIKSa) located on Staphylococcus aureus plasmid pCH91. The toxin (PemKSa) is a sequence-specific endoribonuclease recognizing the tetrad sequence U↓AUU, and the antitoxin (PemISa) inhibits toxin activity by physical interaction. Although the toxin–antitoxin system is responsible for stable plasmid maintenance our data suggest the participation of pemIKSa in global regulation of staphylococcal virulence by alteration of the translation of large pools of genes. We propose a common mechanism of reversible activation of toxin–antitoxin systems based on antitoxin transcript resistance to toxin cleavage. Elucidation of this mechanism is particularly interesting because reversible activation is a prerequisite for the proposed general regulatory role of toxin–antitoxin systems.
Suggested Citation
Michal Bukowski & Robert Lyzen & Weronika M. Helbin & Emilia Bonar & Agnieszka Szalewska-Palasz & Grzegorz Wegrzyn & Grzegorz Dubin & Adam Dubin & Benedykt Wladyka, 2013.
"A regulatory role for Staphylococcus aureus toxin–antitoxin system PemIKSa,"
Nature Communications, Nature, vol. 4(1), pages 1-10, October.
Handle:
RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3012
DOI: 10.1038/ncomms3012
Download full text from publisher
Corrections
All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3012. See general information about how to correct material in RePEc.
If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.
We have no bibliographic references for this item. You can help adding them by using this form .
If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.
For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .
Please note that corrections may take a couple of weeks to filter through
the various RePEc services.