Thermodynamic analysis of the heterodimerization of leucine zippers of Jun and Fos transcription factors

Jun and Fos are components of the AP1 family of transcription factors and bind to the promoters of a diverse multitude of genes involved in critical cellular responses such as cell growth and proliferation, cell cycle regulation, embryonic development and cancer. Here, using the powerful technique o...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2008-10, Vol.375 (4), p.634-638
Main Authors: Seldeen, Kenneth L., McDonald, Caleb B., Deegan, Brian J., Farooq, Amjad
Format: Article
Language:English
Subjects:
60 APPLIED LIFE SCIENCES
bZIP domain
CALORIMETRY
CELL PROLIFERATION
Coupled folding-dimerization
DIMERIZATION
DIMERS
ENTROPY
GENE REGULATION
Humans
Isothermal titration calorimetry
LEUCINE
Leucine zipper thermodynamics
Leucine Zippers
NEOPLASMS
ONTOGENESIS
PROMOTERS
Protein Structure, Tertiary
Proto-Oncogene Proteins c-fos - metabolism
Proto-Oncogene Proteins c-jun - metabolism
SPECIFIC HEAT
Temperature
THERMODYNAMICS
TITRATION
TRANSCRIPTION FACTORS
Transcription factors Jun and Fos
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Summary:Jun and Fos are components of the AP1 family of transcription factors and bind to the promoters of a diverse multitude of genes involved in critical cellular responses such as cell growth and proliferation, cell cycle regulation, embryonic development and cancer. Here, using the powerful technique of isothermal titration calorimetry, we characterize the thermodynamics of heterodimerization of leucine zippers of Jun and Fos. Our data suggest that the heterodimerization of leucine zippers is driven by enthalpic forces with unfavorable entropy change at physiological temperatures. Furthermore, the basic regions appear to modulate the heterodimerization of leucine zippers and may undergo at least partial folding upon heterodimerization. Large negative heat capacity changes accompanying the heterodimerization of leucine zippers are consistent with the view that leucine zippers do not retain α-helical conformations in isolation and that the formation of the native coiled-coil α-helical dimer is attained through a coupled folding-dimerization mechanism.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2008.08.058