The TEA domain is a DNA-binding region of about 66 to 68 amino acids that has been named after the two proteins that originally defined the domain: TEF-1 and abaA. The TEA domain is located toward the amino terminus of eukaryotic transcription factors of the TEA/ATTS family. It is predicted to contain three alpha-helices, two of which have been demonstrated to be important for DNA binding [ (PUBMED:8389695) ].
GO process:
regulation of transcription, DNA-templated (GO:0006355)
Regulation of gene expression at the beginning of mammalian development and the TEAD family of transcription factors.
Dev Genet. 1998; 22: 43-55
Display abstract
In mouse development, transcription is first detected in late 1-cell embryos, but translation of newly synthesized transcripts does not begin until the 2-cell stage. Thus, the onset of zygotic gene expression (ZGE) is regulated at the level of both transcription and translation. Chromatin-mediated repression is established after formation of a 2-cell embryo, concurrent with the developmental acquisition of enhancer function. The most effective enhancer in cleavage stage mouse embryos depends on DNA binding sites for TEF-1, the prototype for a family of transcription factors that share the same TEA DNA binding domain. Mice contain at least four, and perhaps five, genes with the same TEA DNA binding domain (mTEAD genes). Since mTEAD-2 is the only one expressed during the first 7 days of mouse development, it is most likely responsible for the TEAD transcription factor activity that first appears at the beginning of ZGE. All four mTEAD genes are expressed at later embryonic stages and in adult tissues; virtually every tissue expresses at least one family member, consistent with a critical role for TEAD proteins in either cell proliferation or differentiation. The 72-amino acid TEA DNA binding domains in mTEAD-2, 3, and 4 are approximately 99% homologous to the same domain in mTEAD-1, and all four proteins bind specifically to the same DNA sequences in vitro with a Kd value of 16-38 nM DNA. Since TEAD proteins appear to be involved in both activation and repression of different genes and do not appear to be functionally redundant, differential activity of TEAD proteins must result either from association with other proteins or from differential sensitivity to chromatin-packaged DNA binding sites.
The scalloped gene encodes a novel, evolutionarily conserved transcription factor required for sensory organ differentiation in Drosophila.
Genes Dev. 1992; 6: 367-79
Display abstract
The scalloped (sd) gene of Drosophila melanogaster was initially characterized by mutants affecting structures on the wing of the adult fly. The sequence of a cDNA clone of the gene reveals a predicted protein sequence homologous to that of a human transcriptional enhancer factor, TEF-1 (68% identity). The homology includes a sequence motif, the TEA domain, that was shown previously to be a DNA-binding domain of TEF-1. An sd enhancer trap strain expresses the reporter gene in a subset of neuroblasts in the central nervous system and in the peripheral sense organs of the embryo. The reporter gene is later expressed in specific regions of the imaginal discs, including regions of the wing disc destined to become structures defective in viable sd mutants. Later still, expression in the adult brain is restricted to subsets of cells, some in regions involved in the processing of gustatory information. These observations indicate that the sd gene encodes a transcription factor that functions in the regulation of cell-specific gene expression during Drosophila development, particularly in the differentiation of the nervous system.
