Structural motifs and potential sigma homologies in the large subunit of human general transcription factor TFIIE.
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.
Ohkuma
Y
Y
Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, New York 10021.
Sumimoto
H
H
Hoffmann
A
A
Shimasaki
S
S
Horikoshi
M
M
Roeder
R G
RG
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004268:DNA-Binding Proteins / Q000737:chemistry; D006801:Humans; D066298:In Vitro Techniques; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D016415:Sequence Alignment; D014157:Transcription Factors / Q000737:chemistry*; D019473:Transcription Factors, TFII; D014158:Transcription, Genetic; D016335:Zinc Fingers
D004268:DNA-Binding Proteins; D046911:Macromolecular Substances; D014157:Transcription Factors; D019473:Transcription Factors, TFII; C066644:transcription factor TFIIE