Structural motifs and potential a homologies in the large subunit of human general transcription factor TFIIE

Yoshiaki Ohkuma, Hideki Sumimoto, Alexander Hoffmann, Shunichi Shimasaki, Masami Horikoshi, Robert G. Roeder

Research output: Contribution to journalArticlepeer-review

71 Citations (Scopus)

Abstract

THE general transcription factor TFIIE has an essential role in eukaryotic transcription initiation together with RNA polymerase II and other general factors1,2. Human TFIIE consists of two subunits of relative molecular mass 57,000 (TFIIE-α) and 34,000 (TFIIE-β)3-5 and joins the preinitiation complex after RNA polymerase II and TFIIF (ref. 5). Here we report the cloning and structure of a complementary DNA encoding a functional human TFIIE-α. TFIIE-α is necessary for transcription initiation together with TFIIE-β, and recombinant TFIIE-α can fully replace the natural subunit in an in vitro transcription assay. The sequence contains several interesting structural motifs6 (leucine repeat, zinc finger and helix-turn-helix) and sequence similarities to bacterial a factors that suggest direct involvement in the regulation of transcription initiation.

Original languageEnglish
Pages (from-to)398-401
Number of pages4
JournalNature
Volume354
Issue number6352
DOIs
Publication statusPublished - Jan 1 1991
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General

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