Details

Autor(en) / Beteiligte

• Anbanandam, Asokan
• Albarado, Diana C.
• Nguyen, Catherine T.
• Halder, Georg
• Gao, Xiaolian
• Veeraraghavan, Sudha

Titel

Insights into Transcription Enhancer Factor 1 (TEF-1) Activity from the Solution Structure of the TEA Domain

Ist Teil von

• Proceedings of the National Academy of Sciences - PNAS, 2006-11, Vol.103 (46), p.17225-17230

Ort / Verlag

United States: National Academy of Sciences

Erscheinungsjahr

2006

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• 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.