Initiation of eukaryotic mRNA transcription requires melting of promoter DNA with the help of the general transcription factors TFIIE and TFIIH. In higher eukaryotes, the general transcription factor TFIIE consists of two subunits: the large alpha subunit ( IPR002853 ) and the small beta ( IPR003166 ). TFIIE beta has been found to bind to the region where the promoter starts to open to be single-stranded upon transcription initiation by RNA polymerase II. The approximately 120-residue central core domain of TFIIE beta plays a role in double-stranded DNA binding of TFIIE [ (PUBMED:10716934) ].
The TFIIE beta central core DNA-binding domain consists of three helices with a beta hairpin at the C terminus, resembling the winged helix proteins. It shows a novel double-stranded DNA-binding activity where the DNA-binding surface locates on the opposite side to the previously reported winged helix motif by forming a positively charged furrow [ (PUBMED:10716934) ].
This entry represents the conserved amino terminal region of eukaryotic TFIIE-alpha and proteins from archaebacteria (TFE) that are also presumed to be TFIIE-alpha subunits [ (PUBMED:9389475) ].
GO process:
transcription initiation from RNA polymerase II promoter (GO:0006367)
Family alignment:
There are 838 TFIIE domains in 838 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing TFIIE domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with TFIIE domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing TFIIE domain in the selected taxonomic class.
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
Structural motifs and potential sigma homologies in the large subunit of human general transcription factor TFIIE.
Nature. 1991; 354: 398-401
Display abstract
The general transcription factor TFIIE has an essential role in eukaryotic transcription initiation together with RNA polymerase II and other general factors. Human TFIIE consists of two subunits of relative molecular mass 57,000 (TFIIE-alpha) and 34,000 (TFIIE-beta) and joins the preinitiation complex after RNA polymerase II and TFIIF. Here we report the cloning and structure of a complementary DNA encoding a functional human TFIIE-alpha. TFIIE-alpha is necessary for transcription initiation together with TFIIE-beta, and recombinant TFIIE-alpha can fully replace the natural subunit in an in vitro transcription assay. The sequence contains several interesting structural motifs (leucine repeat, zinc finger and helix-turn-helix) and sequence similarities to bacterial sigma factors that suggest direct involvement in the regulation of transcription initiation.
Metabolism (metabolic pathways involving proteins which contain this domain)
This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with TFIIE domain which could be assigned to a KEGG orthologous group, and not all proteins containing TFIIE domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.
