title: The histone H3-like TAF is broadly required for transcription in yeast.
abstract: In yeast cells, independent depletion of TAFs (130, 67, 40, and 19) found specifically in TFIID results in selective effects on transcription, including a common effect on his3 core promoter function. In contrast, depletion of TAF17, which is also present in the SAGA histone acetylase complex, causes a decrease in transcription of most genes. However, TAF17-depleted cells maintain Ace1-dependent activation, and they induce de novo activation by heat shock factor in a manner predominantly associated with the activator, not the core promoter. Thus, TAF17 is broadly, but not universally, required for transcription in yeast, TAF17 depletion and TAF130 depletion each disrupt TFIID integrity yet cause different transcriptional consequences, suggesting that the widespread influence of TAF17 might not be due solely to its function in TFIID.
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
authors.forename: Z
authors.initials: Z
authors.lastname: Moqtaderi
authors.forename: M
authors.initials: M
authors.lastname: Keaveney
authors.forename: K
authors.initials: K
authors.lastname: Struhl
mesh_terms: D015153:Blotting, Western; D002352:Carrier Proteins; D002455:Cell Division / Q000187:drug effects; D019327:Copper Sulfate / Q000494:pharmacology; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D029721:Drosophila Proteins; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism; D015966:Gene Expression Regulation, Fungal / Q000187:drug effects; D005800:Genes, Fungal / Q000235:genetics; D018869:Heat-Shock Response / Q000187:drug effects / Q000235:genetics; D006657:Histones / Q000235:genetics; D007700:Kinetics; D008668:Metallothionein / Q000235:genetics; D012319:RNA Polymerase II / Q000378:metabolism; D012333:RNA, Messenger / Q000032:analysis; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000235:genetics* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid; D016385:TATA Box / Q000235:genetics; D035381:TATA-Binding Protein Associated Factors; D015534:Trans-Activators / Q000235:genetics / Q000502:physiology; D035362:Transcription Factor TFIID; D014157:Transcription Factors / Q000235:genetics / Q000276:immunology / Q000378:metabolism* / Q000502:physiology; D019473:Transcription Factors, TFII / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D014158:Transcription, Genetic / Q000187:drug effects
chemical_list: C500769:CUP1-1 protein, S cerevisiae; C060256:CUP2 protein, S cerevisiae; D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D005656:Fungal Proteins; D006657:Histones; D012333:RNA, Messenger; D029701:Saccharomyces cerevisiae Proteins; C116141:TAF9 protein, S cerevisiae; D035381:TATA-Binding Protein Associated Factors; D015534:Trans-Activators; D035362:Transcription Factor TFIID; D014157:Transcription Factors; D019473:Transcription Factors, TFII; C007121:copper thionein; C084120:e(y)1 protein, Drosophila; D008668:Metallothionein; D012319:RNA Polymerase II; D019327:Copper Sulfate