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

Title1H, 13C, and 15N backbone and side-chain chemical shift assignment of the staphylococcal MazF mRNA interferase.
Publication TypeJournal Article
Year of Publication2011
AuthorsZorzini, V., S. Haesaerts, A. Cheung, R. Loris, and N. A. J. van Nuland
JournalBiomol NMR Assign
Volume5
Issue2
Pagination157-60
Date Published2011 Oct
ISSN1874-270X
KeywordsAmino Acid Sequence, Bacterial Proteins, Bacterial Toxins, Carbon Isotopes, Molecular Sequence Data, Nitrogen Isotopes, Nuclear Magnetic Resonance, Biomolecular, Recombinant Proteins, Ribonucleases, Sequence Alignment, Staphylococcus aureus
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.

DOI10.1007/s12104-010-9290-1
Alternate JournalBiomol NMR Assign
PubMed ID21213075
Grant ListAI076298 / AI / NIAID NIH HHS / United States