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J. Biol. Chem., Vol. 275, Issue 29, 22166-22171, July 21, 2000

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A Conserved Transcription Motif Suggesting Functional Parallels between Caenorhabditis elegans SKN-1 and Cap`n'Collar-related Basic Leucine Zipper Proteins^*

Amy K. Walker, Raymond See^§, Ceri Batchelder, Thip Kophengnavong, J. Timothy Gronniger, Yang Shi^§, and T. Keith Blackwell^§¶

From the  Center for Blood Research and the ^§ Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115

In Caenorhabditis elegans, the predicted transcription factor SKN-1 is required for embryonic endodermal and mesodermal specification and for maintaining differentiated intestinal cells post-embryonically. The SKN-1 DNA-binding region is related to the Cap`n'Collar (CNC) family of basic leucine zipper proteins, but uniquely, SKN-1 binds DNA as a monomer. CNC proteins are absent in C. elegans, however; and their involvement in the endoderm and mesoderm suggests some functional parallels to SKN-1. Using a cell culture assay, we show that SKN-1 induces transcription and contains three potent activation domains. The functional core of one domain is a short motif, the DIDLID element, which is highly conserved in a subgroup of vertebrate CNC proteins. The DIDLID element is important for SKN-1-driven transcription, suggesting a likely significance in other CNC proteins. SKN-1 binds to and activates transcription through the p300/cAMP-responsive element-binding protein-binding protein (CBP) coactivator, supporting the genetic prediction that SKN-1 recruits the C. elegans p300/CBP ortholog, CBP-1. The DIDLID element appears to act independently of p300/CBP, however, suggesting a distinct conserved target. The evolutionarily preservation of the DIDLID transcriptional element supports the model that SKN-1 and some CNC proteins interact with analogous cofactors and may have preserved some similar functions despite having divergent DNA-binding domains.

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