Biochemical characterization of human Ecdysoneless reveals a role in transcriptional regulation
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Jun Hyun Kim
Abstract
Ecdysoneless (Ecd) is an evolutionarily conserved protein and its function is essential for embryonic development in Drosophila and cell growth in yeast. However, its function has remained unknown until recently. Studies in yeast suggested a potential role of Ecd in transcription; however, Ecd lacks a DNA-binding domain. Using a GAL4-luciferase reporter assay and a GAL4 DNA-binding domain fusion with Ecd or its mutants, we present evidence that human Ecd has a transactivation activity in its C-terminal region. Importantly, further analyses using point mutants showed that a single amino acid change at either Asp-484 or Leu-489 essentially completely abolishes the transactivation activity of Ecd. We further demonstrate that Ecd interacts with p300, a histone acetyltransferase, and coexpression of Ecd with p300 enhances the Ecd-mediated transactivation activity. Ecd localizes to both nucleus and cytoplasm and shuttles between the nucleus and cytoplasm; however, it exhibits strong nuclear export. Based on previous yeast studies and evidence provided here, we suggest that Ecd functions as a transcriptional regulator. Our results indicate an important function of human Ecd and provide a basis to explore the transcriptional partners of Ecd.
©2010 by Walter de Gruyter Berlin New York
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Articles in the same Issue
- REVIEW
- Hexose-6-phosphate dehydrogenase in the endoplasmic reticulum
- GENES AND NUCLEIC ACIDS
- Biochemical characterization of human Ecdysoneless reveals a role in transcriptional regulation
- PROTEIN STRUCTURE AND FUNCTION
- Bovine β-lactoglobulin acts as an acid-resistant drug carrier by exploiting its diverse binding regions
- Structural studies of the phosphatidylinositol 3-kinase (PI3K) SH3 domain in complex with a peptide ligand: role of the anchor residue in ligand binding
- A fluorescence correlation spectroscopy study of ligand interaction with cytokinin-specific binding protein from mung bean
- The oxygen-independent coproporphyrinogen III oxidase HemN utilizes harderoporphyrinogen as a reaction intermediate during conversion of coproporphyrinogen III to protoporphyrinogen IX
- MEMBRANES, LIPIDS, GLYCOBIOLOGY
- Phytosphingosine kills Candida albicans by disrupting its cell membrane
- CELL BIOLOGY AND SIGNALING
- Dexamethasone-dependent versus -independent markers of epithelial to mesenchymal transition in primary hepatocytes
- PROTEOLYSIS
- Potential role of multiple members of the kallikrein-related peptidase family of serine proteases in activating latent TGFβ1 in semen
- Binding and activation of the human plasma kinin-forming system on the cell walls of Candida albicans and Candida tropicalis
- A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037
- NOVEL TECHNIQUES
- CYP21-catalyzed production of the long-term urinary metandienone metabolite 17β-hydroxymethyl-17α-methyl-18-norandrosta-1,4,13-trien-3-one: a contribution to the fight against doping
