VapC and VapB are the toxin and anti‐toxin proteins, respectively, of the VapCB toxin–antitoxin system found in bacteria and associated with stunting cell growth during stressful conditions.
Seth P. Jones+4 more
semanticscholar +2 more sources
Protein expression, crystallization and preliminary X-ray crystallographic analysis of the isolated Shigella flexneri VapC toxin. [PDF]
Upon release from the stable complex formed with its antitoxin VapB, the toxin VapC (MvpT) of the Gram-negative pathogen Shigella flexneri is capable of globally down-regulating translation by specifically cleaving initiator tRNA(fMet) in the anticodon ...
Kehan Xu+7 more
semanticscholar +2 more sources
VapCs of Mycobacterium tuberculosis cleave RNAs essential for translation [PDF]
The major human pathogen Mycobacterium tuberculosis can survive in the host organism for decades without causing symptoms. A large cohort of Toxin–Antitoxin (TA) modules contribute to this persistence.
Gerdes, Kenn+3 more
core +3 more sources
Growth and Translation Inhibition through Sequence-specific RNA Binding by Mycobacterium tuberculosis VapC Toxin* [PDF]
Background: Mycobacterium tuberculosis harbors a highly expanded number of toxin-antitoxin (TA) systems. Results: The M. tuberculosis VapC-mt4 toxin blocks translation and arrests growth through RNA binding at a short recognition sequence. Conclusion: M.
Jared D. Sharp+5 more
semanticscholar +2 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 ...
A. P. Y. Lopes+8 more
semanticscholar +3 more sources
Effect of Rickettsial Toxin VapC on Its Eukaryotic Host
Rickettsia are intracellular bacteria typically associated with arthropods that can be transmitted to humans by infected vectors. Rickettsia spp. can cause mild to severe human disease with a possible protection effect of corticosteroids when antibiotic ...
G. Audoly+9 more
semanticscholar +3 more sources
VapC toxins drive cellular dormancy under uranium stress for the extreme thermoacidophile Metallosphaera prunae [PDF]
A. Mukherjee+5 more
semanticscholar +2 more sources
Correction to: Resonance assignments of a VapC family toxin from Clostridium thermocellum
Chen Wang+3 more
semanticscholar +2 more sources
Homologous VapC Toxins Inhibit Translation and Cell Growth by Sequence-Specific Cleavage of tRNAfMet [PDF]
L. Walling, J. Butler
semanticscholar +2 more sources
Crystal structure of PAE0151 from Pyrobaculum aerophilum, a PIN‐domain (VapC) protein from a toxin‐antitoxin operon [PDF]
R. D. Bunker+3 more
semanticscholar +2 more sources