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Science 29 June 1990:
Vol. 248. no. 4963, pp. 1646 - 1650
DOI: 10.1126/science.2194289

Articles

Science, Vol 248, Issue 4963, 1646-1650
Copyright © 1990 by American Association for the Advancement of Science


articles

Cloning of a transcriptionally active human TATA binding factor

CC Kao, PM Lieberman, MC Schmidt, Q Zhou, R Pei, and AJ Berk

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

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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