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Toxin-antitoxin system gene mutations driving Mycobacterium tuberculosis transmission revealed by whole genome sequencing. [PDF]
Hou Y +7 more
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Future Microbiology
Mycobacterium tuberculosis (Mtb) harbors a high number of Toxin-Antitoxin (TA) systems, wherein half of them belong to virulence associated proteins B and C (VapBC) family that has a characteristic PilT N-terminus domain and ribonuclease activity ...
Renu Chaudhary +2 more
exaly +4 more sources
Mycobacterium tuberculosis (Mtb) harbors a high number of Toxin-Antitoxin (TA) systems, wherein half of them belong to virulence associated proteins B and C (VapBC) family that has a characteristic PilT N-terminus domain and ribonuclease activity ...
Renu Chaudhary +2 more
exaly +4 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.
Chuan Wu, Chun Fu Wu
exaly +4 more sources
Crystal structure of proteolyzed VapBC and DNA‐bound VapBC from Salmonella enterica Typhimurium LT2 and VapC as a putative Ca2+‐dependent ribonuclease [PDF]
Bacterial 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 +7 more
semanticscholar +3 more sources
Journal of Structural Biology, 2014
Although PIN (PilT N-terminal)-domain proteins are known to have ribonuclease activity, their specific mechanism of action remains unknown. VapCs form a family of ribonucleases that possess a PIN-domain assembly and are known as toxins. The activities of VapCs are impaired by VapB antitoxins.
Uddipan Das +2 more
exaly +5 more sources
Although PIN (PilT N-terminal)-domain proteins are known to have ribonuclease activity, their specific mechanism of action remains unknown. VapCs form a family of ribonucleases that possess a PIN-domain assembly and are known as toxins. The activities of VapCs are impaired by VapB antitoxins.
Uddipan Das +2 more
exaly +5 more sources
Journal of Medicinal Chemistry, 2020
Klebsiella pneumoniae is one of the most critical opportunistic pathogens. TA systems are promising drug targets because they are related to the survival of bacterial pathogens. However, structural information on TA systems in K.
Sung-Min Kang +4 more
semanticscholar +3 more sources
Klebsiella pneumoniae is one of the most critical opportunistic pathogens. TA systems are promising drug targets because they are related to the survival of bacterial pathogens. However, structural information on TA systems in K.
Sung-Min Kang +4 more
semanticscholar +3 more sources
Shigella flexneri est un pathogène intracellulaire à Gram négatif et l'agent responsable de la dysenterie bacillaire. Sa capacité à envahir les cellules épithéliales et à se disséminer dans les tissus de l'hôte repose sur l'expression finement régulée ...
E. Saifi
semanticscholar +2 more sources
Higher-Order Structure in Bacterial VapBC Toxin-Antitoxin Complexes.
Sub-cellular biochemistry, 2017Toxin-antitoxin systems are widespread in the bacterial kingdom, including in pathogenic species, where they allow rapid adaptation to changing environmental conditions through selective inhibition of key cellular processes, such as DNA replication or protein translation.
K. L. Bendtsen, D. E. Brodersen
semanticscholar +5 more sources

