A M Baranger | PubMed Health

PubMed1998

Accessory factor-bZIP-DNA interactions.

DNA binding and transcriptional activation by basic region leucine zipper (bZIP) proteins can be enhanced by accessory factors. In the past year, three accessory factor-bZIP-DNA complexes have been investigated extensively. Experiments have probed the effect of accessory factors on bZIP-DNA specificity, the residues that participate in stabilizing these complexes, the contribution of DNA conformation to accessory factor-bZIP interactions, and the relative stabilization of bZIP dimerization and DNA binding by accessory factors.

DNA Adducts↗

PubMed1995

Mechanism of DNA-binding enhancement by the human T-cell leukaemia virus transactivator Tax.

Tax protein activates transcription of the human T-cell leukaemia virus type I (HTLV-I) genome through three imperfect cyclic AMP-responsive element (CRE) target sites located within the viral promoter. Previous work has shown that Tax interacts with the bZIP element of proteins that bind the CRE target site to promote peptide dimerization, suggesting an association between Tax and bZIP coiled coil. Here we show that the site of interaction with Tax is not the coiled coil, but the basic segment. This interaction increases the stability of the GCN4 bZIP dimer by 1.7 kcal mol-1 and the DNA affinity of the dimer by 1.9 kcal mol-1. The differential effect of Tax on several bZip-DNA complexes that differ in peptide sequence or DNA conformation suggests a model for Tax action based on stabilization of a distinct DNA-bound protein structure. This model may explain how Tax interacts with transcription factors of considerable sequence diversity to alter patterns of gene expression.

Amino Acid Sequence↗