Linked Life Data

12533537

Source:http://linkedlifedata.com/resource/pubmed/id/12533537

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pubmed-article:12533537pubmed:abstractTextThe Escherichia coli mazEF operon defines a chromosomal addiction module that programs cell death under various stress conditions. It encodes the toxic and long-lived MazF and the labile antidote MazE. The denaturation of MazE is a two-state reversible dimer-monomer transition. At lower concentrations the denatured state is significantly populated. This leads to a new aspect of the regulation of MazE concentration, which may decide about the life and death of the cell. Interactions of MazE with a dromedary antibody domain, cAbMaz1 (previously used as a crystallization aid), as well as with promoter DNA were studied using microcalorimetric and spectroscopic techniques. Unique features of cAbMaz1 enable a specific enthalpy-driven recognition of MazE and, thus, a significant stabilization of its dimeric native conformation. The MazE dimer and the MazE dimer-cAbMaz1 complex show very similar binding characteristics with promoter DNA, i.e. three binding sites with apparent affinities in micromolar range and highly exothermic binding accompanied by large negative entropy contributions. A working model for the MazE-DNA assembly is proposed on the basis of the structural and binding data. Both binding and stability studies lead to a picture of MazE solution structure that is significantly more unfolded than the structure observed in a crystal of the MazE-cAbMaz1 complex.lld:pubmed
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pubmed-article:12533537pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:12533537pubmed:articleTitleRecognition of the intrinsically flexible addiction antidote MazE by a dromedary single domain antibody fragment. Structure, thermodynamics of binding, stability, and influence on interactions with DNA.lld:pubmed
pubmed-article:12533537pubmed:affiliationDepartment of Ultrastructure, Vrije Universiteit Brussel, Paardenstraat 65, B-1640 St. Genesius Rode, Belgium. jurij.lah@uni-lj.silld:pubmed
pubmed-article:12533537pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12533537pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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