1. Academic Validation
  2. Cloning of a transcriptionally active human TATA binding factor

Cloning of a transcriptionally active human TATA binding factor

  • Science. 1990 Jun 29;248(4963):1646-50. doi: 10.1126/science.2194289.
C C Kao 1 P M Lieberman M C Schmidt Q Zhou R Pei A J Berk
Affiliations

Affiliation

  • 1 Department of Microbiology, Molecular Biology Institute, University of California, Los Angeles 90024-1570.
Abstract

Transcription factor IID (TFIID) binds to the TATA box promoter element and regulates the expression of most eukaryotic genes transcribed by RNA polymerase II. Complementary DNA (cDNA) encoding a human TFIID protein has been cloned. The human TFIID polypeptide has 339 Amino acids and a molecular size of 37,745 daltons. The carboxyl-terminal 181 Amino acids of the human TFIID protein shares 80% identity with the TFIID protein from Saccharomyces cerevisiae. The amino terminus contains an unusual repeat of 38 consecutive glutamine residues and an X-Thr-Pro repeat. Expression of DNA in reticulocyte lysates or in Escherichia coli yielded a protein that was competent for both DNA binding and transcription activation.

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