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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : Biochemistry

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Biochemistry - 18 Aug 1998

Terenzi H, Alzari PM, Zakin MM

Link to Pubmed [PMID] – 9708984

Biochemistry 1998 Aug;37(33):11488-95

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.

http://www.ncbi.nlm.nih.gov/pubmed/9708984