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1H, 13C, and 15N backbone and side-chain chemical shift assignment of the staphylococcal MazF mRNA interferase

Authors :
Sarah Haesaerts
Remy Loris
Valentina Zorzini
Nico A. J. van Nuland
Ambrose L. Cheung
Ultrastructure
Structural Biology Brussels
Department of Bio-engineering Sciences
Source :
Vrije Universiteit Brussel
Publication Year :
2011
Publisher :
Springer Science and Business Media LLC, 2011.

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 (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.

Details

ISSN :
1874270X and 18742718
Volume :
5
Database :
OpenAIRE
Journal :
Biomolecular NMR Assignments
Accession number :
edsair.doi.dedup.....2fce53ad7c30dd1c61c1e12aa943c960
Full Text :
https://doi.org/10.1007/s12104-010-9290-1