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

Tubon TC, Tansey WP, Herr W
Mol Cell Biol. 2004 24 (7): 2863-74

PMID: 15024075 · PMCID: PMC371104 · 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 (TFIIB(ZR)) and a carboxy-terminal core (TFIIB(CORE)). 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 TFIIB(ZR) 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 TFIIB(ZR) surface is directly involved in the recruitment of pol II to a TATA box-containing promoter. Curiously, although the amino-terminal human TFIIB(ZR) 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 recruitment-has changed in sequence specificity during eukaryotic evolution.

MeSH Terms (17)

Amino Acid Sequence Animals Gene Expression Regulation HeLa Cells Humans Models, Molecular Molecular Sequence Data Mutation Promoter Regions, Genetic Protein Structure, Secondary Protein Structure, Tertiary RNA Polymerase II Saccharomyces cerevisiae Proteins Sequence Alignment Transcription, Genetic Transcription Factor TFIIB Zinc

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