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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

Abstract : 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.
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Submitted on : Tuesday, February 9, 2021 - 7:28:37 PM
Last modification on : Thursday, April 1, 2021 - 3:21:51 AM

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Hernan Terenzi, Pedro Alzari, Mario 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, American Chemical Society, 1998, 37 (33), pp.11488-11495. ⟨10.1021/bi980748i⟩. ⟨pasteur-03136652⟩

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