Results 11 to 20 of about 1,206 (173)

Regulation of the vapBC-1 toxin-antitoxin locus in nontypeable Haemophilus influenzae. [PDF]

open access: goldPLoS ONE, 2012
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]

open access: hybridRNA, 2021
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

VapC from the leptospiral VapBC toxin-antitoxin module displays ribonuclease activity on the initiator tRNA.

open access: goldPLoS ONE, 2014
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]

open access: goldNucleic Acids Research, 2012
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]

open access: bronzeJournal of Bacteriology, 2019
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]

open access: hybridJournal of Biological Chemistry, 2009
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]

open access: closedActa Crystallographica Section A Foundations and Advances, 2021
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]

open access: bronzeProtein Engineering Design and Selection, 2011
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]

open access: bronzeCell Research, 2004
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]

open access: bronzeFEMS Microbiology Letters, 2014
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

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