ERH (Enhancer of Rudimentary Homologue), a Conserved Factor Identical between Frog and Human, Is a Transcriptional Repressor
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E. Pogge von Strandmann
Abstract
Drosophila enhancer of rudimentary [e(r)] interacts genetically with the rudimentary gene, which encodes a protein possessing the first three enzymatic activities of the pyrimidine biosynthesis pathway. A regulatory or enzymatic activity of e(r) in pyrimidine biosynthesis and the cell cycle has been suggested, but nothing is known about its molecular function. The factor is evolutionarily highly conserved since homologues exist in plants and mammals. We cloned the Xenopus enhancer of rudimentary homologue (XERH) as an interaction partner of DCoH/PCD (dimerisation cofactor of HNF1/pterin-4 carbinolamine dehydratase) in the yeast twohybrid assay. DCoH/PCD is a multifunctional factor originally identified as a positive cofactor of the HNF1 homeobox transcription factors. XERH is a 104 amino acid protein that is identical to its mammalian homologues. The mRNA is expressed maternally, enriched in ectodermal derivatives during development and ubiquitously detectable in the adult. Fused to the DNA binding region of the GAL4 transcription factor domain, XERH represses the activity of a GAL4 responsive reporter in HeLa, but not in NIH3T3 cells. Furthermore, the DCoH/PCD coactivation of a HNF1 responsive reporter is inhibited by XERH. We propose that XERH is a cell typespecific transcriptional repressor, probably interfering with HNF1-dependent gene regulation via DCoH/PCD.
Copyright © 2001 by Walter de Gruyter GmbH & Co. KG
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- Evolution in Silico and in Vitro: The RNA Model
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- The Stochastic Evolution of Catalysts in Spatially Resolved Molecular Systems
- Fragment-Based Flexible Ligand Docking by Evolutionary Optimization
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Articles in the same Issue
- Highlight: Evolution in Vivo, in Vitro and in Machina
- Modeling Genetic Networks and Their Evolution: A Complex Dynamical Systems Perspective
- Evolution in Silico and in Vitro: The RNA Model
- Divergent Evolution of (??)8-Barrel Enzymes
- RNA-Catalyzed Carbon-Carbon Bond Formation
- Toward Automated Nucleic Acid Enzyme Selection
- Duocalins: Engineered Ligand-Binding Proteins with Dual Specificity Derived from the Lipocalin Fold
- The Stochastic Evolution of Catalysts in Spatially Resolved Molecular Systems
- Fragment-Based Flexible Ligand Docking by Evolutionary Optimization
- Specific Nucleoprotein Complexes within Adenovirus Capsids
- ERH (Enhancer of Rudimentary Homologue), a Conserved Factor Identical between Frog and Human, Is a Transcriptional Repressor
- Signal Transduction by the Chemokine Receptor CXCR5: Structural Requirements for G Protein Activation Analyzed by Chimeric CXCR1/CXCR5 Molecules
- Arginine-Specific Cysteine Proteinase from Porphyromonas gingivalis as a Convenient Tool in Protein Chemistry
- Chemokine-Induced Secretion of Gelatinase B in Primary Human Monocytes
