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Distinct Mutations in Yeast TAF_II25 Differentially Affect the Composition of TFIID and SAGA Complexes as Well as Global Gene Expression Patterns

Doris B. Kirschner,^1, Elmar vom Baur,¹ Christelle Thibault,¹ Steven L. Sanders,^2, Yann-Gaël Gangloff,^1, Irwin Davidson,¹ P. Anthony Weil,² and Làszlò Tora^1*

Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, F-67404 Illkirch Cedex, CU de Strasbourg, France,¹ Department of Molecular Physiology & Biophysics, Vanderbilt University School of Medicine, Nashville, Tennessee²

Received 23 July 2001/ Returned for modification 10 September 2001/ Accepted 31 January 2002

The RNA polymerase II transcription factor TFIID, composed of the TATA-binding protein (TBP) and TBP-associated factors (TAF_IIs), nucleates preinitiation complex formation at protein-coding gene promoters. SAGA, a second TAF_II-containing multiprotein complex, is involved in transcription regulation in Saccharomyces cerevisiae. One of the essential protein components common to SAGA and TFIID is yTAF_II25. We define a minimal evolutionarily conserved 91-amino-acid region of TAF_II25 containing a histone fold domain that is necessary and sufficient for growth in vivo. Different temperature-sensitive mutations of yTAF_II25 or chimeras with the human homologue TAF_II30 arrested cell growth at either the G₁ or G₂/M cell cycle phase and displayed distinct phenotypic changes and gene expression patterns. Immunoprecipitation studies revealed that TAF_II25 mutation-dependent gene expression and phenotypic changes correlated at least partially with the integrity of SAGA and TFIID. Genome-wide expression analysis revealed that the five TAF_II25 temperature-sensitive mutant alleles individually affect the expression of between 18 and 33% of genes, whereas taken together they affect 64% of all class II genes. Thus, different yTAF_II25 mutations induce distinct phenotypes and affect the regulation of different subsets of genes, demonstrating that no individual TAF_II mutant allele reflects the full range of its normal functions.

Present address: Institut Curie, UMR 218 du CNRS, 75248 Paris Cedex 05, France.

Present address: Wellcome/CRC Institute and Department of Pathology, University of Cambridge, Cambridge CB2 1QR, United Kingdom.

Present address: Friedrich Miescher Institute, CH-4002 Basel, Switzerland.

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