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Structural features involved in the formation of a complex between the monomeric or the dimeric form of the rev-erb beta DNA-binding domain and its DNA reactive sites.

Authors
  • Terenzi, H
  • Alzari, P M
  • Zakin, M M
Type
Published Article
Journal
Biochemistry
Publication Date
Aug 18, 1998
Volume
37
Issue
33
Pages
11488–11495
Identifiers
PMID: 9708984
Source
Medline
License
Unknown

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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