Peter Weil
Faculty Member
Last active: 11/4/2015

Identification and characterization of a TFIID-like multiprotein complex from Saccharomyces cerevisiae.

Poon D, Bai Y, Campbell AM, Bjorklund S, Kim YJ, Zhou S, Kornberg RD, Weil PA
Proc Natl Acad Sci U S A. 1995 92 (18): 8224-8

PMID: 7667272 · PMCID: PMC41129 · DOI:10.1073/pnas.92.18.8224

Although the mechanisms of transcriptional regulation by RNA polymerase II are apparently highly conserved from yeast to man, the identification of a yeast TATA-binding protein (TBP)-TBP-associated factor (TAFII) complex comparable to the metazoan TFIID component of the basal transcriptional machinery has remained elusive. Here, we report the isolation of a yeast TBP-TAFII complex which can mediate transcriptional activation by GAL4-VP16 in a highly purified yeast in vitro transcription system. We have cloned and sequenced the genes encoding four of the multiple yeast TAFII proteins comprising the TBP-TAFII multisubunit complex and find that they are similar at the amino acid level to both human and Drosophila TFIID subunits. Using epitope-tagging and immunoprecipitation experiments, we demonstrate that these genes encode bona fide TAF proteins and show that the yeast TBP-TAFII complex is minimally composed of TBP and seven distinct yTAFII proteins ranging in size from M(r) = 150,000 to M(r) = 25,000. In addition, by constructing null alleles of the cloned TAF-encoding genes, we show that normal function of the TAF-encoding genes is essential for yeast cell viability.

MeSH Terms (10)

Amino Acid Sequence Animals Cloning, Molecular Genes, Fungal Humans Molecular Sequence Data Saccharomyces cerevisiae Sequence Homology, Amino Acid Transcription Factors Transcription Factor TFIID

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