Structural highlights
Function
[MAZF_STAAW] Toxic component of a toxin-antitoxin (TA) module. Ribosome-independent, sequence-specific endoribonuclease that cleaves mRNA, thus inhibiting protein synthesis and inducing bacterial stasis. Cleavages occur preferentially in a U-rich region with a consensus sequence of 5'-[ACG]UU[ACG]-3' in single-stranded RNA (By similarity).
Publication Abstract from PubMed
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 (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
- ↑ Zorzini V, Haesaerts S, Cheung A, Loris R, van Nuland NA. 1H, 13C, and 15N backbone and side-chain chemical shift assignment of the staphylococcal MazF mRNA interferase. Biomol NMR Assign. 2011 Oct;5(2):157-60. doi: 10.1007/s12104-010-9290-1. Epub, 2011 Jan 7. PMID:21213075 doi:http://dx.doi.org/10.1007/s12104-010-9290-1
