2019
DOI: 10.1038/s41589-018-0216-z
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Mechanism of regulation and neutralization of the AtaR–AtaT toxin–antitoxin system

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Cited by 37 publications
(45 citation statements)
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“…f Time courses of the acetylation of Met-tRNAf Met variants with mutations in the bottom half of the three consecutive G-C pairs in a. g Quantification of the acetylation efficiencies in f, as in e. The bars in the graph are SD of three independent (n = 3) experiments, and the data are presented as mean values ± SD. respectively 20,21 . The loop between α3 and β4 in AtaTb and α1 in AtaTa form the path for the 3′-end of tRNA to enter the catalytic site and interact with the 3′-single-stranded region of tRNAf Met (Fig.…”
Section: Resultsmentioning
confidence: 99%
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“…f Time courses of the acetylation of Met-tRNAf Met variants with mutations in the bottom half of the three consecutive G-C pairs in a. g Quantification of the acetylation efficiencies in f, as in e. The bars in the graph are SD of three independent (n = 3) experiments, and the data are presented as mean values ± SD. respectively 20,21 . The loop between α3 and β4 in AtaTb and α1 in AtaTa form the path for the 3′-end of tRNA to enter the catalytic site and interact with the 3′-single-stranded region of tRNAf Met (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…The crystal belongs to the space group P2 1 2 1 2 and contains eight AtaT molecules and two Ac-Met-tRNAf Met molecules in the asymmetric unit. The initial phase was determined by the molecular replacement method, using the AtaT homodimer (PDB: 6GTP) 20 and tRNAf Met structures in the structure of the complex of Met-tRNAf Met formyltransferase and formyl-Met-tRNAf Met (PDB: 2FMT) 24 as search models. The structure was model-built and refined to an R factor of 28.6% (R free = 34.1%) at 3.8 Å resolution.…”
Section: Resultsmentioning
confidence: 99%
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“…Structures are colored in rainbow from N-terminus (blue) to C-terminus (red), in cases of dimers the second monomer is in gray. Structures were visualized using ChimeraX, PDB codes were following: E. coli MazF:3nfc; E. coli HicAB:6hpb (Manav et al, 2019); S. oneidensis SO_3166-SO3165 (HEPN): 5yep (Jia et al, 2018); H. pylori HP0315 (VapD): 3ui3 (Kwon et al, 2012); S. flexneri VapC D7A : 5ecw (Xu et al, 2016); E. coli RelE R81A,R83A : 2kc9 (Li et al, 2009); E. coli HipA S150A : 3tpb (Schumacher et al, 2012); E. coli AtaT Y 144F : 6gtp (Jurenas et al, 2019); prophage P1 Phd-Doc: 3k33 (Garcia-Pino et al, 2010). In the cases of structures in complexes with antitoxin, the coordinates of antitoxin were deleted.…”
Section: Mazf Toxinsmentioning
confidence: 99%
“…This leaves the toxins to exert their toxic effects, which leads to growth arrest and dormancy.” [ 4 ] Hence, it is common to assume a protease degrading antitoxin bound to toxin is the means to activate toxins. [ 70–72 ] We suggest that the current model of reactivation of toxins in this manner is unlikely and unsupported in that to the best of our knowledge, there are no reports showing the degradation of antitoxins bound to toxins in vitro or in vivo. Hence, it seems this paradigm has been established, like cell killing, without experimental evidence.…”
Section: Reviewmentioning
confidence: 96%