You are hereBiblio / Energetics of structural transitions of the addiction antitoxin MazE: is a programmed bacterial cell death dependent on the intrinsically flexible nature of the antitoxins?
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 ArticleSource:
Volume 280, Issue 17, p.17397 - 17407 (2005)URL:
PM:15735309Keywords:
Antitoxins; chemistry; Apoptosis; Calorimetry; Differential Scanning; Circular Dichroism; Crystallography; X-Ray; DNA-Binding Proteins; Dimerization; Endoribonucleases; Escherichia coli; metabolism; Escherichia coli Proteins; Fluorometry; Heat; Hydrogen-IonAbstract:
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
Notes:
DA - 20050425
IS - 0021-9258 (Print)
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
RN - 0 (Antitoxins)
RN - 0 (DNA-Binding Proteins)
RN - 0 (Escherichia coli Proteins)
RN - 0 (MazE protein, E coli)
RN - 0 (MazF protein, E coli)
RN - 57-13-6 (Urea)
RN - EC 3.1.- (Endoribonucleases)
SB - IM