Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain.

Publication Date



Proc Natl Acad Sci U S A. 2006 November 14; 103(46): 17225–17230


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.


Amino Acid Sequence, Animals, Base Sequence, DNA, DNA-Binding Proteins, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Phylogeny, Protein Binding, Protein Structure, Tertiary, Sequence Alignment, Transcription Factors