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

ABSTRACT: 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.

SUBMITTER: Anbanandam A

PROVIDER: S-EPMC1859914 | biostudies-literature | 2006 Nov

REPOSITORIES: biostudies-literature

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

Anbanandam Asokan A Albarado Diana C DC Nguyen Catherine T CT Halder Georg G Gao Xiaolian X Veeraraghavan Sudha S

Proceedings of the National Academy of Sciences of the United States of America 20061103 46

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 mic ...[more]

PMID: 17085591

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