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rdf:type |
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lifeskim:mentions |
umls-concept:C0003295,
umls-concept:C0012854,
umls-concept:C0013127,
umls-concept:C0039808,
umls-concept:C0085281,
umls-concept:C0205171,
umls-concept:C0205360,
umls-concept:C0443220,
umls-concept:C0524637,
umls-concept:C0678594,
umls-concept:C1167622,
umls-concept:C1514562,
umls-concept:C1566673,
umls-concept:C1704675,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
16
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pubmed:dateCreated |
2003-4-14
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pubmed:abstractText |
The 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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14101-11
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12533537-Amino Acid Sequence,
pubmed-meshheading:12533537-Animals,
pubmed-meshheading:12533537-Binding Sites,
pubmed-meshheading:12533537-Biochemistry,
pubmed-meshheading:12533537-Calorimetry,
pubmed-meshheading:12533537-Calorimetry, Differential Scanning,
pubmed-meshheading:12533537-Camels,
pubmed-meshheading:12533537-Circular Dichroism,
pubmed-meshheading:12533537-DNA,
pubmed-meshheading:12533537-DNA-Binding Proteins,
pubmed-meshheading:12533537-Dimerization,
pubmed-meshheading:12533537-Entropy,
pubmed-meshheading:12533537-Escherichia coli,
pubmed-meshheading:12533537-Escherichia coli Proteins,
pubmed-meshheading:12533537-Immunoglobulin Fragments,
pubmed-meshheading:12533537-Models, Molecular,
pubmed-meshheading:12533537-Molecular Sequence Data,
pubmed-meshheading:12533537-Peptides,
pubmed-meshheading:12533537-Promoter Regions, Genetic,
pubmed-meshheading:12533537-Protein Binding,
pubmed-meshheading:12533537-Protein Conformation,
pubmed-meshheading:12533537-Protein Structure, Secondary,
pubmed-meshheading:12533537-Protein Structure, Tertiary,
pubmed-meshheading:12533537-Sequence Homology, Amino Acid,
pubmed-meshheading:12533537-Temperature,
pubmed-meshheading:12533537-Thermodynamics,
pubmed-meshheading:12533537-Time Factors
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pubmed:year |
2003
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pubmed:articleTitle |
Recognition 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.
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pubmed:affiliation |
Department of Ultrastructure, Vrije Universiteit Brussel, Paardenstraat 65, B-1640 St. Genesius Rode, Belgium. jurij.lah@uni-lj.si
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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