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

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 le...

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Published in:The Journal of biological chemistry 2000-07, Vol.275 (29), p.22166-22171
Main Authors: Walker, Amy K., See, Raymond, Batchelder, Ceri, Kophengnavong, Thip, Gronniger, J.Timothy, Shi, Yang, Blackwell, T.Keith
Format: Article
Language:English
Subjects:
Animals
Caenorhabditis elegans
Caenorhabditis elegans - genetics
Caenorhabditis elegans Proteins
Cap 'n' collar protein
DNA-Binding Proteins - genetics
Drosophila Proteins
Helminth Proteins - genetics
Leucine Zippers - genetics
Repressor Proteins - genetics
SKN-1 protein
Transcription Factors - genetics
Transcription, Genetic
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Summary: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 theC. 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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M001746200