Regulation of the vapBC-1 toxin-antitoxin locus in nontypeable Haemophilus influenzae. [PDF]
Nontypeable Haemophilus influenzae (NTHi) are human-adapted commensal bacteria that can cause a number of chronic mucosal infections, including otitis media and bronchitis.
Susan D Cline +2 more
doaj +10 more sources
Identification and characterization of VapBC toxin-antitoxin system in Bosea sp. PAMC 26642 isolated from Arctic lichens. [PDF]
Toxin–antitoxin (TA) systems are genetic modules composed of a toxin interfering with cellular processes and its cognate antitoxin, which counteracts the activity of the toxin. TA modules are widespread in bacterial and archaeal genomes.
Jeon H, Choi E, Hwang J.
europepmc +6 more sources
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 ...
Alexandre P Y Lopes +8 more
doaj +6 more sources
Regulation of Enteric vapBC Transcription: Induction by VapC Toxin Dimer-Breaking [PDF]
Toxin-antitoxin (TA) loci encode inhibitors of translation, replication or cell wall synthesis and are common elements of prokaryotic plasmids and chromosomes.
K. Winther, K. Gerdes
semanticscholar +7 more sources
Crystal Structure of VapBC-1 from Nontypeable Haemophilus influenzae and the Effect of PIN Domain Mutations on Survival during Infection [PDF]
Herein the crystal structure of the VapBC-1 complex from nontypeable Haemophilus influenzae (NTHi) is described. Our results show that some of the mutations in the PIN domain of the VapC-1 toxin were associated with decreased toxicity in E. coli, but the
A. L. Molinaro +6 more
semanticscholar +5 more sources
Structure and Proposed Activity of a Member of the VapBC Family of Toxin-Antitoxin Systems [PDF]
In prokaryotes, cognate toxin-antitoxin pairs have long been known, but no three-dimensional structure has been available for any given complex from Mycobacterium tuberculosis.
L. Miallau +6 more
semanticscholar +4 more sources
Investigation of possible tolerance mutations in a VapBC toxin–antitoxin system through structure determination [PDF]
Bacterial chromosomes contain large numbers of toxin-antitoxin (TA) systems, consisting of a gene encoding a toxic protein and a gene encoding an antitoxin which can be an RNA or a protein [1, 2]. In the largest known group of type II TA systems, vapBC ,
M. R. Nielsen, D. Brodersen
semanticscholar +3 more sources
The PIN-domain ribonucleases and the prokaryotic VapBC toxin-antitoxin array. [PDF]
The PIN-domains are small proteins of ~130 amino acids that are found in bacteria, archaea and eukaryotes and are defined by a group of three strictly conserved acidic amino acids. The conserved three-dimensional structures of the PIN-domains cluster these acidic residues in an enzymatic active site. PIN-domains cleave single-stranded RNA in a sequence-
V. Arcus +3 more
semanticscholar +5 more sources
Characterization of a novel toxin-antitoxin module, VapBC, encoded by Leptospira interrogans chromosome [PDF]
Comparative genomic analysis of the coding sequences (CDSs) of Leptospira interrogans revealed a pair of closely linked genes homologous to the vapBC loci of many other bacteria with respect to both deduced amino acid sequences and operon organizations.
Yi Zhang +6 more
semanticscholar +4 more sources
Toxin-antitoxin vapBC locus participates in formation of the dormant state in Mycobacterium smegmatis. [PDF]
Toxin-antitoxin (TA) loci are widely spread in bacterial plasmids and chromosomes. Toxins affect important functions of bacterial cells such as translation, replication and cell-wall synthesis, whereas antitoxins are toxin inhibitors. Participation in formation of the dormant state in bacteria is suggested to be a possible function of toxins.
O. I. Demidenok +2 more
semanticscholar +4 more sources

