Title | Energetics of structural transitions of the addiction antitoxin MazE: is a programmed bacterial cell death dependent on the intrinsically flexible nature of the antitoxins? |
Publication Type | Journal Article |
Year of Publication | 2005 |
Authors | Lah, J., M. Simic, G. Vesnaver, I. Marianovsky, G. Glaser, H. Engelberg-Kulka, and R. Loris |
Journal | J Biol Chem |
Volume | 280 |
Issue | 17 |
Pagination | 17397-407 |
Date Published | 2005 Apr 29 |
ISSN | 0021-9258 |
Keywords | Antitoxins, Apoptosis, Calorimetry, Differential Scanning, Circular Dichroism, Crystallography, X-Ray, Dimerization, DNA-Binding Proteins, Endoribonucleases, Escherichia coli, Escherichia coli Proteins, Fluorometry, Hot Temperature, Hydrogen-Ion Concentration, Models, Molecular, Protein Conformation, Protein Folding, Protein Structure, Secondary, Spectrometry, Fluorescence, Spectrophotometry, Temperature, Thermodynamics, Ultraviolet Rays, Urea |
Abstract | The Escherichia coli mazEF addiction module plays a crucial role in the cell death program that is triggered under various stress conditions. It codes for the toxin MazF and the antitoxin MazE, which interferes with the lethal action of the toxin. To better understand the role of various conformations of MazE in bacterial life, its order-disorder transitions were monitored by differential scanning calorimetry, spectropolarimetry, and fluorimetry. The changes in spectral and thermodynamic properties accompanying MazE dimer denaturation can be described in terms of a compensating reversible process of the partial folding of the unstructured C-terminal half (high mean net charge, low mean hydrophobicity) and monomerization coupled with the partial unfolding of the structured N-terminal half (low mean net charge, high mean hydrophobicity). At pH |
DOI | 10.1074/jbc.M501128200 |
Alternate Journal | J. Biol. Chem. |
PubMed ID | 15735309 |
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