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The Basic Amino Acid-Rich DNA-Binding Element of the NF-IL6 Transcription Factor Contains Two Functionally Distinct
Allan R. Brasier1, Amalendra Kumar
1Division of Endocrinology, Department of Internal Medicine, University of Texas Medical Branch, Galveston, USA and Division of Endocrinology, Department of Human Biological Chemistry and Genetics, and the Sealy Center for Molecular Sciences, University of Texas Medical Branch, Galveston, USA.
Abstract:
Nuclear factor-interleukin-6 (NF-IL6), a human transcription factor of the CCAAT-box/enhancer binding protein (C/EBP) family, is widely implicated as a "master regulator" of hepatic acute-phrase response and inflammatory cytokine gene expression. NF-IL6 contains, at its N-terminus, an alanine- and proline-rich transactivation domain, followed at the C-terminus by a basic domain-leucine zipper (bZIP) DNA-binding motif. Understanding how the NF-IL6 transcription factor interacts with DNA is fundamental to its role as a transactivator because sequence-specific DNA-binding is prerequisite to promoter activation. We review our findings on the identification of the minimal "core" DNA-binding domain and the discovery of a novel bZIP element that influences DNA-binding kinetics. Manipulation of this domain allows for design of molecules that can be used as competitive antagonists or targeted delivery of molecules to selected regions of the eukaryotic genome.