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Molecular and genetic characterization of a Taf1p domain essential for yeast TFIID assembly
Journal article   Peer reviewed

Molecular and genetic characterization of a Taf1p domain essential for yeast TFIID assembly

Madhu V Singh, Christin E Bland and P Anthony Weil
Molecular and cellular biology, Vol.24(11), pp.4929-4942
06/2004
DOI: 10.1128/MCB.24.11.4929-4942.2004
PMCID: PMC416396
PMID: 15143185
url
http://doi.org/10.1128/MCB.24.11.4929-4942.2004View
Open Access

Abstract

Yeast Taf1p is an integral component of the multiprotein transcription factor TFIID. By using coimmunoprecipitation assays, coupled with a comprehensive set of deletion mutants encompassing the entire open reading frame of TAF1, we have discovered an essential role of a small portion of yeast Taf1p. This domain of Taf1p, termed region 4, consisting of amino acids 200 to 303, contributes critically to the assembly and stability of the 15-subunit TFIID holocomplex. Region 4 of Taf1p is mutationally sensitive, can assemble several Tafps into a partial TFIID complex, and interacts directly with Taf4p and Taf6p. Mutations in Taf1p-region 4 induce temperature-conditional growth of yeast cells. At the nonpermissive temperature these mutations have drastic effects on both TFIID integrity and mRNA synthesis. These data are consistent with the hypothesis that Taf1p subserves a critical scaffold function within the TFIID complex. The significance of these data with regard to TFIID structure and function is discussed.
Mutation TATA-Binding Protein Associated Factors - metabolism Transcription Factor TFIID - chemistry Temperature Saccharomyces cerevisiae - genetics Protein Structure, Tertiary - genetics Saccharomyces cerevisiae Proteins - genetics Transcription Factor TFIID - metabolism TATA-Binding Protein Associated Factors - genetics Saccharomyces cerevisiae - metabolism Transcription Factor TFIID - genetics Transcription Factor TFIID - biosynthesis Saccharomyces cerevisiae Proteins - metabolism Protein Structure, Tertiary - physiology

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