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Title

Toxin ζ Reduces the ATP and Modulates the Uridine Diphosphate-N-acetylglucosamine Pool

AuthorsMoreno-del Álamo, María ; Tabone, Mariangela; Muñoz-Martínez, Juan; Valverde, José R. ; Alonso, Juan C.
KeywordsToxin-antitoxin system
Cell wall inhibition
Bacterial persistence
Nucleotide hydrolysis
Uridine diphosphate-N-acetylglucosamine
Issue Date9-Jan-2019
PublisherMultidisciplinary Digital Publishing Institute
CitationToxins 11(1): 29 (2019)
AbstractToxin ζ expression triggers a reversible state of dormancy, diminishes the pool of purine nucleotides, promotes (p)ppGpp synthesis, phosphorylates a fraction of the peptidoglycan precursor uridine diphosphate-N-acetylglucosamine (UNAG), leading to unreactive UNAG-P, induces persistence in a reduced subpopulation, and sensitizes cells to different antibiotics. Here, we combined computational analyses with biochemical experiments to examine the mechanism of toxin ζ action. Free ζ toxin showed low affinity for UNAG. Toxin ζ bound to UNAG hydrolyzed ATP·Mg<sup>2+</sup>, with the accumulation of ADP, P<sub>i</sub>, and produced low levels of phosphorylated UNAG (UNAG-P). Toxin ζ, which has a large ATP binding pocket, may temporally favor ATP binding in a position that is distant from UNAG, hindering UNAG phosphorylation upon ATP hydrolysis. The residues D67, E116, R158 and R171, involved in the interaction with metal, ATP, and UNAG, were essential for the toxic and ATPase activities of toxin ζ; whereas the E100 and T128 residues were partially dispensable. The results indicate that ζ bound to UNAG reduces the ATP concentration, which indirectly induces a reversible dormant state, and modulates the pool of UNAG.
Publisher version (URL)http://dx.doi.org/10.3390/toxins11010029
URIhttp://hdl.handle.net/10261/176147
DOI10.3390/toxins11010029
ISSN2072-6651
Appears in Collections:(CNB) Artículos
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