Evidence for a non-alpha-helical DNA-binding motif in the Rel homology region. | Zendy

J Liu | Zendy; Mikiko Sodeoka | Zendy; W S Lane | Zendy; Gregory L. Verdine | Zendy

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Evidence for a non-alpha-helical DNA-binding motif in the Rel homology region.

Author(s) -

J Liu,

Mikiko Sodeoka,

W S Lane,

Gregory L. Verdine

Publication year - 1994

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.91.3.908

Subject(s) - biology , sequence motif , dna , genetics , homology (biology) , binding site , peptide sequence , dna binding protein , amino acid , transcription factor , microbiology and biotechnology , gene

The Rel family of transcription factors serve as terminal messengers in a variety of developmental and receptor-mediated signaling pathways. These proteins are related by a domain of approximately 280 amino acids, the Rel homology region, which mediates dimerization and sequence-specific binding to DNA. Here we report the use of photocrosslinking and site-directed mutagenesis to identify specific contact partners in a Rel protein-DNA interface. Within the Rel homology region of NF-kappa B p50 (also known as KBF1), two amino acid residues were identified by photocrosslinking to adjacent bases in a beta-interferon regulatory element. Secondary structure analysis suggests that the DNA-binding motif of the Rel homology region comprises a beta-turn-beta structure, in contrast to the alpha-helical motifs so commonly observed in transcription factors.

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