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  The ng_ζ1 toxin of the gonococcal epsilon/zeta toxin/antitoxin system drains precursors for cell wall synthesis

Rocker, A., Peschke, M., Kittilä, T., Sakson, R., Brieke, C., & Meinhart, A. (2018). The ng_ζ1 toxin of the gonococcal epsilon/zeta toxin/antitoxin system drains precursors for cell wall synthesis. Nature Communications, 9: 1686, pp. 1-11. doi:10.1038/s41467-018-03652-8.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0001-3D52-F Version Permalink: https://hdl.handle.net/21.11116/0000-0001-3D53-E
Genre: Journal Article

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 Creators:
Rocker, Andrea1, Author           
Peschke, Madeleine1, Author           
Kittilä, Tiia1, Author           
Sakson, Roman1, Author           
Brieke, Clara1, Author           
Meinhart, Anton1, Author           
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: Enzyme mechanisms ; Pathogens ; X-ray crystallography
 Abstract: Bacterial toxin–antitoxin complexes are emerging as key players modulating bacterial physiology as activation of toxins induces stasis or programmed cell death by interference with vital cellular processes. Zeta toxins, which are prevalent in many bacterial genomes, were shown to interfere with cell wall formation by perturbing peptidoglycan synthesis in Gram-positive bacteria. Here, we characterize the epsilon/zeta toxin–antitoxin (TA) homologue from the Gram-negative pathogen Neisseria gonorrhoeae termed ng_ɛ1 / ng_ζ1. Contrary to previously studied streptococcal epsilon/zeta TA systems, ng_ɛ1 has an epsilon-unrelated fold and ng_ζ1 displays broader substrate specificity and phosphorylates multiple UDP-activated sugars that are precursors of peptidoglycan and lipopolysaccharide synthesis. Moreover, the phosphorylation site is different from the streptococcal zeta toxins, resulting in a different interference with cell wall synthesis. This difference most likely reflects adaptation to the individual cell wall composition of Gram-negative and Gram-positive organisms but also the distinct involvement of cell wall components in virulence.

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Language(s): eng - English
 Dates: 2017-10-012018-03-022018-04-27
 Publication Status: Published online
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-018-03652-8
 Degree: -

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 9 Sequence Number: 1686 Start / End Page: 1 - 11 Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723