Dissecting the role of leucine zippers in the binding of bZIP domains of Jun transcription factor to DNA.

Leucine zippers, structural motifs typically comprised of five successive heptads of amino acids with a signature leucine at every seventh position, play a central role in the dimerization of bZIP family of transcription factors and their subsequent binding to the DNA promoter regions of target genes. Herein, using analytical laser scattering (ALS) in combination with isothermal titration calorimetry (ITC), we study the effect of successive C-terminal truncation of leucine zippers on the dimerization and energetics of binding of bZIP domains of Jun transcription factor to its DNA response element. Our data show that all five heptads are critical for the dimerization of bZIP domains and that the successive C-terminal truncation of residues leading up to each signature leucine significantly compromises the binding of bZIP domains to DNA. Taken together, our study provides novel insights into the energetic contributions of leucine zippers to the binding of bZIP domains of Jun transcription factor to DNA.

Seldeen KL ，McDonald CB ，Deegan BJ ，Bhat V ，Farooq A ... -  《-》

Coupling of folding and DNA-binding in the bZIP domains of Jun-Fos heterodimeric transcription factor.

Seldeen KL ，McDonald CB ，Deegan BJ ，Farooq A ... -  《-》

Single nucleotide variants of the TGACTCA motif modulate energetics and orientation of binding of the Jun-Fos heterodimeric transcription factor.

Seldeen KL ，McDonald CB ，Deegan BJ ，Farooq A ... -  《-》

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

Seldeen KL ，McDonald CB ，Deegan BJ ，Farooq A ... -  《-》

DNA plasticity is a key determinant of the energetics of binding of Jun-Fos heterodimeric transcription factor to genetic variants of TGACGTCA motif.

Seldeen KL ，McDonald CB ，Deegan BJ ，Bhat V ，Farooq A ... -  《-》