Abstract
MazF proteins are ribonucleases that cleave mRNA with high sequence-specificity as part of bacterial stress response and that are neutralized by the action of the corresponding antitoxin MazE. Prolonged activation of the toxin MazF leads to cell death. Several mazEF modules from Gram-negative bacteria have been characterized in terms of catalytic activity, auto-regulation mechanism and structure, but less is known about their distant relatives found in Gram-positive organisms. Currently, no solution NMR structure is available for any wild-type MazF toxin. Here we report the 1H, 15N and 13C backbone and side-chain chemical shift assignments of this toxin from the pathogen bacterium Staphylococcus aureus. The BMRB accession number is 17288.
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Acknowledgments
This work was supported by NIH grant AI076298 and by grants from FWO, OZR-VUB and VIB. V.Z. acknowledges receipt of PhD grant from the Onderzoeksraad of the VUB. We thank Niles Donegan and Zhibiao Fu for producing the pETDuet1 construct.
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Zorzini, V., Haesaerts, S., Cheung, A. et al. 1H, 13C, and 15N backbone and side-chain chemical shift assignment of the staphylococcal MazF mRNA interferase. Biomol NMR Assign 5, 157–160 (2011). https://doi.org/10.1007/s12104-010-9290-1
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DOI: https://doi.org/10.1007/s12104-010-9290-1