Results 141 to 150 of about 1,080 (170)
Enteric virulence associated protein VapC inhibits translation by cleavage of initiator tRNA [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 2011 Eukaryotic PIN (PilT N-terminal) domain proteins are ribonucleases involved in quality control, metabolism and maturation of mRNA and rRNA. The majority of prokaryotic PIN-domain proteins are encoded by the abundant vapBC toxin—antitoxin loci and inhibit translation by an unknown mechanism ...
Kristoffer Skovbo Winther +2 more
exaly +6 more sources
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VapC toxin switches M. smegmatis cells into dormancy through 23S rRNA cleavage
Archives of Microbiology, 2022Mycobacterium tuberculosis is an extremely successful pathogen known for its ability to cause latent infection. The latter is connected with the bacterium resting state development and is considered to be based on the activity of toxin-antitoxin (TA) systems at least in part.
Mikhail Shumkov +2 more
exaly +3 more sources
Growth-regulating Mycobacterium tuberculosis VapC-mt4 toxin is an isoacceptor-specific tRNase [PDF]
Nature Communications, 2015 Toxin-antitoxin (TA) systems are implicated in the downregulation of bacterial cell growth associated with stress survival and latent tuberculosis infection, yet the activities and intracellular targets of these TA toxins are largely uncharacterized. Here, we use a specialized RNA-seq approach to identify targets of a Mycobacterium tuberculosis VapC TA
Bryce E Nickels +2 more
exaly +3 more sources
Growth and Translation Inhibition through Sequence-specific RNA Binding by Mycobacterium tuberculosis VapC Toxin [PDF]
Journal of Biological Chemistry, 2012 The Mycobacterium tuberculosis genome harbors an unusually large number of toxin-antitoxin (TA) modules. Curiously, over half of these are VapBC (virulence-associated protein) family members. Nonetheless, the cellular target, precise mode of action, and physiological role of the VapC toxins in this important pathogen remain unclear.
Robert Husson +2 more
exaly +3 more sources
Resonance assignments of a VapC family toxin from Clostridium thermocellum
Biomolecular NMR Assignments, 2016Toxin-antitoxin (TA) systems widely exist in bacterial plasmids, phages, and chromosomes and play important roles in growth persistence and host-pathogen interaction. Virulence associated protein BC (VapBC) family TAs are the most abundant TAs in bacteria and many pathogens contain a large number of vapBC loci in the genome which have been extensively ...
Chen Wang +3 more
openaire +2 more sources
VapC toxin inhibition as a method for prevention of the formation of resting forms of mycobacteria
Applied Biochemistry and Microbiology, 2016It has been shown that inactivation of the VapC toxin from the VapВС toxin-antitoxin system prevents mycobacterial cells from transitioning to an ovoid state that meets the criteria of dormancy. The results indicate a potential target for medicines that prevent the development of latent tuberculosis infection and provide a basis to obtain bacterial ...
O I, Demidenok +2 more
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Are all VapC toxins of Mycobacterium tuberculosis endowed with enigmatic RNase activity?
Journal of BiosciencesMycobacterium tuberculosis (M. tb) employs an extensive network of more than 90 toxin-antitoxin systems, and among them, VapC toxins are the most abundant. While most VapCs function as classical RNases with toxic effects, a significant number of them do not exhibit toxicity.
Seyed E Hasnain +2 more
exaly +3 more sources
Structure-Based De Novo Design of Mycobacterium Tuberculosis VapC-Activating Stapled Peptides
ACS Chemical Biology, 2020Toxin-antitoxin (TA) systems have been considered essential factors for bacterial survival. During our drug development program aimed against tuberculosis (TB), we discovered certain peptides that mimic the binding of the VapBC30 complex, leading to the arrest of bacterial cell growth and eventually cell death.
Sung-Min Kang +5 more
openaire +2 more sources
Structural analysis of the active site architecture of the VapC toxin from
ABSTRACTThe VapC toxin from the Shigella flexneri 2a virulence plasmid pMYSH6000 belongs to the PIN domain protein family, which is characterized by a conserved fold with low amino acid sequence conservation. The toxin is a bona fide Mg2+‐dependent ribonuclease and has been shown to target initiator tRNAfMet in vivo. Here, we present crystal structures
Xu, Kehan +2 more
openaire +3 more sources