A nonconserved surface of the TFIIB zinc ribbon domain plays a direct role in RNA polymerase II recruitment

Tubon, T. C., Tansey, W. P., Herr, W. (April 2004) A nonconserved surface of the TFIIB zinc ribbon domain plays a direct role in RNA polymerase II recruitment. Molecular and Cellular Biology, 24 (7). pp. 2863-2874. ISSN 0270-7306

URL: http://mcb.asm.org/cgi/content/full/24/7/2863?maxt...
DOI: 10.1128/MCB.24.7.2863-2874.2004


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 promoters-pol II recruitmenthas changed in sequence specificity during eukaryotic evolution.

Item Type: Paper
Uncontrolled Keywords: GENERAL TRANSCRIPTION FACTORS general transcription factors START SITE SELECTION start site selection TATA-BINDING TATA binding PROTEIN N-TERMINAL REGION n-terminal region PREINITIATION COMPLEX preinitiation complex IN-VIVO in-vivo YEAST TFIIB yeast DNA-BINDING DNA binding DEPENDENT TRANSCRIPTION dependent transcription FUNCTIONAL DOMAINS functional domains
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor
CSHL Authors:
Depositing User: CSHL Librarian
Date: April 2004
Date Deposited: 17 Jan 2012 17:00
Last Modified: 17 Jan 2012 17:00
URI: https://repository.cshl.edu/id/eprint/22507

Actions (login required)

Administrator's edit/view item Administrator's edit/view item
CSHL HomeAbout CSHLResearchEducationNews & FeaturesCampus & Public EventsCareersGiving