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  Assembly dynamics and stability of the pneumococcal epsilon zeta antitoxin toxin (PezAT) system from Streptococcus pneumoniae

Mutschler, H., Reinstein, J., & Meinhart, A. (2010). Assembly dynamics and stability of the pneumococcal epsilon zeta antitoxin toxin (PezAT) system from Streptococcus pneumoniae. The Journal of Biological Chemistry, 285(28), 21797-21806. doi:10.1074/jbc.M110.126250.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-1FC3-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-1FC4-4
Genre: Journal Article
Alternative Title : Assembly dynamics and stability of the pneumococcal epsilon zeta antitoxin toxin (PezAT) system from Streptococcus pneumoniae

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 Creators:
Mutschler, Hannes1, Author              
Reinstein, Jochen1, Author              
Meinhart, Anton1, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: Bacterial Toxins ; Cell Death ; Enzyme Inhibitors ; Protein Assembly ; Protein-Protein Interactions ; Toxin Antitoxin Systems ; Assembly Kinetics
 Abstract: The pneumococcal epsilon zeta antitoxin toxin (PezAT) system is a chromosomally encoded, class II toxin antitoxin system from the human pathogen Streptococcus pneumnoniae. Neutralization of the bacteriotoxic protein PezT is carried out by complex formation with its cognate antitoxin PezA. Here we study the stability of the inhibitory complex in vivo and in vitro. We found that toxin release is impeded in Escherichia coli and Bacillus subtilis due to the proteolytic resistance of PezA once bound to PezT. These findings are supported by in vitro experiments demonstrating a strong thermodynamic stabilization of both proteins upon binding. A detailed kinetic analysis of PezAT assembly revealed that these particular features of PezAT are based on a strong, electrostatically guided binding mechanism leading to a stable toxin antitoxin complex with femtomolar affinity. Our data show that PezAT complex formation is distinct to all other conventional toxin antitoxin modules and a controlled mode of toxin release is required for activation.

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Language(s): eng - English
 Dates: 2010-03-242010-05-042010-07-09
 Publication Status: Published in print
 Pages: 21
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 664589
DOI: 10.1074/jbc.M110.126250
URI: http://www.ncbi.nlm.nih.gov/pubmed/20442221
Other: 7575
 Degree: -

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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 285 (28) Sequence Number: - Start / End Page: 21797 - 21806 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1