Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain
| Autor: | Diana C. Albarado, Asokan Anbanandam, Catherine T. Nguyen, Sudha Veeraraghavan, Georg Halder, Xiaolian Gao |
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| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular Molecular Sequence Data Biology DNA-binding protein Transcription (biology) Animals Humans Amino Acid Sequence Binding site Enhancer TEAD1 Transcription factor Nuclear Magnetic Resonance Biomolecular Phylogeny Regulation of gene expression Genetics Multidisciplinary Base Sequence DNA Biological Sciences Cell biology Protein Structure Tertiary DNA-Binding Proteins Homeobox Sequence Alignment Protein Binding Transcription Factors |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 103(46) |
| ISSN: | 0027-8424 |
| Popis: | Transcription enhancer factor 1 is essential for cardiac, skeletal, and smooth muscle development and uses its N-terminal TEA domain (TEAD) to bind M-CAT elements. Here, we present the first structure of TEAD and show that it is a three-helix bundle with a homeodomain fold. Structural data reveal how TEAD binds DNA. Using structure-function correlations, we find that the L1 loop is essential for cooperative loading of TEAD molecules on to tandemly duplicated M-CAT sites. Furthermore, using a microarray chip-based assay, we establish that known binding sites of the full-length protein are only a subset of DNA elements recognized by TEAD. Our results provide a model for understanding the regulation of genome-wide gene expression during development by TEA/ATTS family of transcription factors. |
| Databáze: | OpenAIRE |
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