Biomolecular NMR Assignments

, Volume 5, Issue 2, pp 157–160

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

  • Valentina Zorzini
  • Sarah Haesaerts
  • Ambrose Cheung
  • Remy Loris
  • Nico A. J. van Nuland
Article

DOI: 10.1007/s12104-010-9290-1

Cite this article as:
Zorzini, V., Haesaerts, S., Cheung, A. et al. Biomol NMR Assign (2011) 5: 157. doi:10.1007/s12104-010-9290-1
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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.

Keywords

Toxin-antitoxin moduleMacromolecular complexNMRMazFStaphylococcus aureus

Copyright information

© Springer Science+Business Media B.V. 2011

Authors and Affiliations

  • Valentina Zorzini
    • 1
    • 2
  • Sarah Haesaerts
    • 1
    • 2
  • Ambrose Cheung
    • 3
  • Remy Loris
    • 1
    • 2
  • Nico A. J. van Nuland
    • 1
    • 2
  1. 1.Structural Biology BrusselsVrije Universiteit Brussel (VUB)BrusselsBelgium
  2. 2.Department of Molecular and Cellular InteractionsVIBBrusselsBelgium
  3. 3.Department of Microbiology and ImmunologyDartmouth Medical SchoolHanoverUSA