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Molecular and Cellular Biology, April 2004, p. 2863-2874, Vol. 24, No. 7
0270-7306/04/$08.00+0 DOI: 10.1128/MCB.24.7.2863-2874.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Graduate Program in Genetics, State University of New York at Stony Brook, Stony Brook, New York 11794,1 Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 117242
Received 4 August 2003/ Returned for modification 30 September 2003/ Accepted 7 January 2004
The general transcription factor TFIIB is a highly conserved and essential component of the eukaryotic RNA polymerase II (pol II) transcription initiation machinery. It consists of a single polypeptide with two conserved structural domains: an amino-terminal zinc ribbon structure (TFIIBZR) and a carboxy-terminal core (TFIIBCORE). We have analyzed the role of the amino-terminal region of human TFIIB in transcription in vivo and in vitro. We identified a small nonconserved surface of the TFIIBZR that is required for pol II transcription in vivo and for different types of basal pol II transcription in vitro. Consistent with a general role in transcription, this TFIIBZR surface is directly involved in the recruitment of pol II to a TATA box-containing promoter. Curiously, although the amino-terminal human TFIIBZR domain can recruit both human pol II and yeast (Saccharomyces cerevisiae) pol II, the yeast TFIIB amino-terminal region recruits yeast pol II but not human pol II. Thus, a critical process in transcription from many different promoterspol II recruitmenthas changed in sequence specificity during eukaryotic evolution.
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