2mf2
Structural and biophysical characterization of the mRNA interferase SaMazF from Staphylococcus aureus.Structural and biophysical characterization of the mRNA interferase SaMazF from Staphylococcus aureus.
Structural highlights
FunctionMAZF_STAA8 Toxic component of a type II toxin-antitoxin (TA) system. Ribosome-independent, sequence-specific endoribonuclease that cleaves mRNA, thus inhibiting protein synthesis and inducing bacterial stasis. It cuts between the first and nucleotides of 5'-UACAU-3' in single-stranded RNA. Neutralized by coexpression with cognate antitoxin MazE.[UniProtKB:A6QIR4] Publication Abstract from PubMedMazF 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 (1)H, (15)N and (13)C backbone and side-chain chemical shift assignments of this toxin from the pathogen bacterium Staphylococcus aureus. The BMRB accession number is 17288. 1H, 13C, and 15N backbone and side-chain chemical shift assignment of the staphylococcal MazF mRNA interferase.,Zorzini V, Haesaerts S, Cheung A, Loris R, van Nuland NA Biomol NMR Assign. 2011 Oct;5(2):157-60. doi: 10.1007/s12104-010-9290-1. Epub, 2011 Jan 7. PMID:21213075[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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