Results 111 to 120 of about 756 (133)
Identification of a VapBC toxin–antitoxin system in a thermophilic bacterium Thermus thermophilus HB27 [PDF]
Extremophiles, 2016 There are 12 putative toxin-antitoxin (TA) loci in the Thermus thermophilus HB27 genome, including four VapBC and three HicBA families. Expression of these seven putative toxin genes in Escherichia coli demonstrated that one putative VapC toxin TTC0125 and two putative HicA toxins, TTC1395 and TTC1705, inhibited cell growth, and co-expression with ...
Yu-Qi Fan, T. Hoshino, A. Nakamura
semanticscholar +4 more sources
The PIN-domain ribonucleases and the prokaryotic VapBC toxin-antitoxin array. [PDF]
Protein 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
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Toxin-antitoxin vapBC locus participates in formation of the dormant state in Mycobacterium smegmatis. [PDF]
FEMS 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
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Environmental microbiology, 2014
The symbiotic nitrogen-fixing soil bacterium Sinorhizobium meliloti carries a large number of toxin-antitoxin (TA) modules both on the chromosome and megaplasmids. One of them, the vapBC-5 module that belongs to the type II systems was characterized here. It encodes an active toxin vapC-5, and was shown to be controlled negatively by the complex of its
Justine Lipuma +7 more
semanticscholar +5 more sources
The symbiotic nitrogen-fixing soil bacterium Sinorhizobium meliloti carries a large number of toxin-antitoxin (TA) modules both on the chromosome and megaplasmids. One of them, the vapBC-5 module that belongs to the type II systems was characterized here. It encodes an active toxin vapC-5, and was shown to be controlled negatively by the complex of its
Justine Lipuma +7 more
semanticscholar +5 more sources
Crystal structure of VapBC from Salmonella typhimurium
, 2020Bacterial toxin-antitoxin (TA) system has gained attention for its essential roles in cellular maintenance and survival under harsh environmental conditions such as nutrient deficiency and antibiotic treatment.
D. Park, B. Lee
semanticscholar +1 more source
Journal of Molecular Biology, 2009
The largest family of bacterial toxin-antitoxin (TA) modules is formed by the vapBC operons, and these are grouped together by virtue of their toxin components belonging to the PilT N-terminal domain family of proteins that are thought to function as ribonucleases.
Jennifer R Robson +4 more
semanticscholar +4 more sources
The largest family of bacterial toxin-antitoxin (TA) modules is formed by the vapBC operons, and these are grouped together by virtue of their toxin components belonging to the PilT N-terminal domain family of proteins that are thought to function as ribonucleases.
Jennifer R Robson +4 more
semanticscholar +4 more sources
Estudos sobre o módulo toxina-antitoxina VapBC 1 de >i/i< sorovar Copenhageni
D. Damiano
semanticscholar +2 more sources
Crystal structure of DNA bound VapBC from Salmonella typhimurium
, 2020D. Park, B. Lee
semanticscholar +1 more source
Structure of VapBC from Shigella sonnei
, 2020S. Lea, S. Hollingshead
semanticscholar +1 more source
Featured System Toxin-antitoxin VapBC-5
Protein Structure Initiative Structural Genomics Knowledgebase, 2009openaire +1 more source