VapC from the leptospiral VapBC toxin-antitoxin module displays ribonuclease activity on the initiator tRNA.
The prokaryotic ubiquitous Toxin-Antitoxin (TA) operons encode a stable toxin and an unstable antitoxin. The most accepted hypothesis of the physiological function of the TA system is the reversible cessation of cellular growth under stress conditions. The major TA family, VapBC is present in the sp...
Main Authors: | Alexandre P Y Lopes, Luana M Lopes, Tatiana R Fraga, Rosa M Chura-Chambi, André L Sanson, Elisabeth Cheng, Erika Nakajima, Ligia Morganti, Elizabeth A L Martins |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2014-01-01
|
Series: | PLoS ONE |
Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25047537/?tool=EBI |
Similar Items
-
VapC toxins from Mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate VapB antitoxins.
by: Bintou Ahmadou Ahidjo, et al.
Published: (2011-01-01) -
Toxin-antitoxin loci <it>vapBC-1</it> and <it>vapXD</it> contribute to survival and virulence in nontypeable <it>Haemophilus influenzae</it>
by: Ren Dabin, et al.
Published: (2012-11-01) -
<i>In Silico</i> Analysis of Genetic VapC Profiles from the Toxin-Antitoxin Type II VapBC Modules among Pathogenic, Intermediate, and Non-Pathogenic <i>Leptospira</i>
by: Alexandre P. Y. Lopes, et al.
Published: (2019-02-01) -
VapC21 Toxin Contributes to Drug-Tolerance and Interacts With Non-cognate VapB32 Antitoxin in Mycobacterium tuberculosis
by: Arun Sharma, et al.
Published: (2020-09-01) -
Characterization of the Deep-Sea Streptomyces sp. SCSIO 02999 Derived VapC/VapB Toxin-Antitoxin System in Escherichia coli
by: Yunxue Guo, et al.
Published: (2016-07-01)