Results 131 to 140 of about 721 (155)

Identification of a VapBC toxin–antitoxin system in a thermophilic bacterium Thermus thermophilus HB27

Identification of a VapBC toxin–antitoxin system in a thermophilic bacterium Thermus thermophilus HB27
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A VapBC Toxin-Antitoxin Module Is a Posttranscriptional Regulator of Metabolic Flux in Mycobacteria [PDF]

Journal of Bacteriology, 2012
ABSTRACT The largest family of toxin-antitoxin (TA) modules are encoded by the vapBC operons, but their roles in bacterial physiology remain enigmatic. Microarray analysis in Mycobacterium smegmatis overexpressing VapC/VapBC revealed a high percentage of downregulated genes with ...
Michael Berney, Paul P Gardner, Vickery L Arcuș   +2 more
exaly   +6 more sources

Crystal structure of the VapBC-15 complex from Mycobacterium tuberculosis reveals a two-metal ion dependent PIN-domain ribonuclease and a variable mode of toxin–antitoxin assembly

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, Vivian Pogenberg, Matthias Wilmanns   +2 more
exaly   +5 more sources

Characterization of a novel toxin-antitoxin module, VapBC, encoded by Leptospira interrogans chromosome [PDF]

Cell 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.
Chuan Wu, Bi Bo
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Regulation of Enteric vapBC Transcription: Induction by VapC Toxin Dimer-Breaking

Nucleic 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. Ten TA loci of Escherichia coli K-12 encode mRNases that cumulatively contribute to persistence (multidrug tolerance) of the bacterial cells. The mechanisms underlying induction and reversion of
Kristoffer Skovbo Winther, Kenn Gerdes, Gerdes Kenn   +2 more
exaly   +4 more sources

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Structural and Functional Study of the Klebsiella pneumoniae VapBC Toxin–Antitoxin System, Including the Development of an Inhibitor That Activates VapC

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. pneumoniae remains lacking; therefore, it is necessary to explore this information for the development of antibacterial ...
Sung-Min Kang, Chenglong Jin, Do-Hee Kim, Yuno Lee, Bong-Jin Lee   +4 more
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Deciphering the role of VapBC toxin-antitoxin systems in Mycobacterium tuberculosis stress adaptation

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. Functional insights into Mtb VapBC TA modules unraveled their role in adaptation to various host-mediated ...
Zoozeal Thakur, Renu Chaudhary, Promod K Mehta   +2 more
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The vapBC Operon from Mycobacterium smegmatis Is An Autoregulated Toxin–Antitoxin Module That Controls Growth via Inhibition of Translation

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.
Robson, Jennifer, McKenzie, Joanna L., Cursons, Ray, Cook, Gregory M., Arcus, Vickery L.   +4 more
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The crystal structure of the Rv0301-Rv0300 VapBC-3 toxin-antitoxin complex from M. tuberculosis reveals a Mg²⁺ ion in the active site and a putative RNA-binding site.

Protein science : a publication of the Protein Society, 2013
VapBC pairs account for 45 out of 88 identified toxin-antitoxin (TA) pairs in the Mycobacterium tuberculosis (Mtb) H37Rv genome. A working model suggests that under times of stress, antitoxin molecules are degraded, releasing the toxins to slow the metabolism of the cell, which in the case of VapC toxins is via their RNase activity.
Andrew B, Min, Linda, Miallau, Michael R, Sawaya, Jeff, Habel, Duilio, Cascio, David, Eisenberg   +5 more
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Transcriptional regulation and functional role of VapBC type II toxin-antitoxin system in Shigella flexneri virulence

Régulation transcriptionnelle et rôle fonctionnel du système toxine-antitoxine VapBC de type II dans la virulence de Shigella flexneri 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
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