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

Kenneth L. Seldeen, Caleb B. McDonald, Brian J. Deegan, Amjad Farooq

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)634-638
Number of pages5
JournalBiochemical and biophysical research communications
Volume375
Issue number4
DOIs
StatePublished - Oct 31 2008

Keywords

  • bZIP domain
  • Coupled folding-dimerization
  • Isothermal titration calorimetry
  • Leucine zipper thermodynamics
  • Transcription factors Jun and Fos

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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