Structural Features Involved in the Formation of a Complex between the Monomeric or the Dimeric Form of the Rev-erbβ DNA-Binding Domain and Its DNA Reactive Sites

Hernan Terenzi (1) , Pedro M. Alzari (2) , Mario M. Zakin (1)

1 Expression des gènes eucaryotes
2 Biochimie Structurale

The nuclear receptor superfamily comprises a group of transcriptional regulators involved in a wide variety of physiological responses. Rev-erb beta is a member of a growing subfamily of orphan nuclear receptors that bind DNA with high affinity either as monomers or as hetero- or homodimers. DNA bending assays, high-resolution footprinting, molecular modeling, and site-directed mutagenesis were used to analyze the structural features of the interaction between the DNA-binding domain (DBD) of the nuclear receptor Rev-erb beta and its DNA target sites. The results obtained point to the involvement of a carboxyl-terminal sequence adjacent to the second zinc finger of the Rev-erb beta DBD in protein-DNA interaction as a monomer or in protein-DNA and protein-protein interactions as a homodimer. They also provide insight about the amino acid residues directly involved in protein-protein contacts.

Domaines: Cristallographie; Biologie structurale [q-bio.BM]; Biochimie, Biologie Moléculaire; Bio-informatique [q-bio.QM]; Biophysique [physics.bio-ph]; Biologie cellulaire

Hernan Terenzi, Pedro M. Alzari, Mario M. Zakin. Structural Features Involved in the Formation of a Complex between the Monomeric or the Dimeric Form of the Rev-erbβ DNA-Binding Domain and Its DNA Reactive Sites. Biochemistry, 1998, 37 (33), pp.11488-11495. ⟨10.1021/bi980748i⟩. ⟨pasteur-03136652⟩