title: Yeast and human TFIIDs are interchangeable for the response to acidic transcriptional activators in vitro.
abstract: Previous work showed that human TFIID fails to support yeast cell growth, although it is nearly identical to yeast TFIID in a carboxy-terminal region of the molecule that suffices for basal, TATA-element-dependent transcription in vitro. These and other findings raised the possibility that TFIID participates in species-specific interactions, possibly with mediator factors, required for activated transcription. Here, we report that human TFIID and amino-terminally truncated derivatives of yeast TFIID are fully functional in support of both basal transcription and the response to acidic activator proteins in a yeast in vitro transcription system. Conversely, and in contrast to previously published results, yeast TFIID supports both basal and activated transcription in reactions reconstituted with human components. This functional interchangeability of yeast and human TFIIDs argues strongly against species specificity with regard to TFIID function in basal transcription and the response to acidic activator proteins. In addition, our results suggest that any intermediary factors between acidic activators and TFIID are conserved from yeast to man.
authors.affiliation: Department of Cell Biology, Stanford University School of Medicine, California 94305.
authors.forename: R J
authors.initials: RJ
authors.lastname: Kelleher
authors.forename: P M
authors.initials: PM
authors.lastname: Flanagan
authors.forename: D I
authors.initials: DI
authors.lastname: Chasman
authors.forename: A S
authors.initials: AS
authors.lastname: Ponticelli
authors.forename: K
authors.initials: K
authors.lastname: Struhl
authors.forename: R D
authors.initials: RD
authors.lastname: Kornberg
mesh_terms: D015152:Blotting, Northern; D002373:Cyclic AMP Receptor Protein / Q000378:metabolism; D004268:DNA-Binding Proteins; D005656:Fungal Proteins / Q000235:genetics; D006801:Humans; D010446:Peptide Fragments / Q000378:metabolism; D011494:Protein Kinases; D012319:RNA Polymerase II / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins; D015534:Trans-Activators / Q000235:genetics; D035362:Transcription Factor TFIID; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic / Q000502:physiology*
chemical_list: D002373:Cyclic AMP Receptor Protein; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; C052130:GAL4 protein, S cerevisiae; C070633:Gal-VP16; D010446:Peptide Fragments; D029701:Saccharomyces cerevisiae Proteins; D015534:Trans-Activators; D035362:Transcription Factor TFIID; D014157:Transcription Factors; D011494:Protein Kinases; D012319:RNA Polymerase II