English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
 Local TagsRelease HistoryDetailsSummary
  A cis-acting antitoxin domain within the chromosomal toxin–antitoxin module EzeT of Escherichia coli quenches toxin activity

Rocker, A., & Meinhart, A. (2015). A cis-acting antitoxin domain within the chromosomal toxin–antitoxin module EzeT of Escherichia coli quenches toxin activity. Molecular Microbiology, 97(3), 589-560. doi:10.1111/mmi.13051.

Item is

 

show all hide all

Basic

show hide
Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0027-9C70-2 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0028-2A79-1
Genre: Journal Article

Files

show Files
hide Files
:
MolMicrobiol_epub_2015_051.pdf (Any fulltext), 8MB
 
File Permalink:
-
Name:
MolMicrobiol_epub_2015_051.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
MolMicrobiol_epub_2015_051_Suppl.pdf (Any fulltext), 2MB
 
File Permalink:
-
Name:
MolMicrobiol_epub_2015_051_Suppl.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Locator:
http://onlinelibrary.wiley.com/doi/10.1111/mmi.13051/epdf (Any fulltext)
Description:
-
OA-Status:
Locator:
http://dx.doi.org/10.1111/mmi.13051 (Any fulltext)
Description:
-
OA-Status:
Locator:
http://onlinelibrary.wiley.com/store/10.1111/mmi.13051/asset/supinfo/mmi13051-sup-0001-si.pdf?v=1&s=abf899ff6a42b947a7cab67159c98149340958b3 (Supplementary material)
Description:
-
OA-Status:

Creators

show
hide
 Creators:
Rocker, Andrea1, Author           
Meinhart, Anton1, Author           
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

Content

show
hide
Free keywords: -
 Abstract: Toxin-antitoxin (TA) systems are widespread genetic modules in the genomes of bacteria and archaea emerging as key players that modulate bacterial physiology. They consist of two parts, a toxic component that blocks an essential cellular process and an antitoxin that inhibits this toxic activity during normal growth. According to the nature of the antitoxin and the mode of inhibition, TA systems are subdivided into different types. Here, we describe the characterization of a type II-like TA system in Escherichia coli called EzeT. While in conventional type II systems the antitoxin is expressed in trans to form an inactive protein-protein complex, EzeT consists of two domains combining toxin and cis-acting antitoxin functionalities in a single polypeptide chain. We show that the C-terminal domain of EzeT is homologous to zeta toxins and is toxic in vivo. The lytic phenotype could be attributed to UDP-N-acetylglucosamine phosphorylation, so far only described for type II epsilon/zeta systems from Gram-positive streptococci. Presence of the N-terminal domain inhibits toxicity in vivo and strongly attenuates kinase activity. Autoinhibition by a cis-acting antitoxin as described here for EzeT-type TA systems can explain the occurrence of single or unusually large toxins, further expanding our understanding of the TA system network

Details

show
hide
Language(s): eng - English
 Dates: 2015-06-062015-06-062015-08-01
 Publication Status: Issued
 Pages: 16
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: Other: 8084
DOI: 10.1111/mmi.13051
URI: http://www.ncbi.nlm.nih.gov/pubmed/25943309
URI: http://onlinelibrary.wiley.com/doi/10.1111/mmi.13051/full
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Molecular Microbiology
  Other : Mol. Microbiol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Oxford : Blackwell Science
Pages: - Volume / Issue: 97 (3) Sequence Number: - Start / End Page: 589 - 560 Identifier: ISSN: 0950-382X
CoNE: https://pure.mpg.de/cone/journals/resource/954925574950