Yeast and human TFIIDs are interchangeable for the response to acidic transcriptional activators in vitro
- PMID: 1310667
- DOI: 10.1101/gad.6.2.296
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.
Similar articles
-
The Gcn4p activation domain interacts specifically in vitro with RNA polymerase II holoenzyme, TFIID, and the Adap-Gcn5p coactivator complex.Mol Cell Biol. 1998 Mar;18(3):1711-24. doi: 10.1128/MCB.18.3.1711. Mol Cell Biol. 1998. PMID: 9488488 Free PMC article.
-
An activator binding module of yeast RNA polymerase II holoenzyme.Mol Cell Biol. 1999 Apr;19(4):2967-76. doi: 10.1128/MCB.19.4.2967. Mol Cell Biol. 1999. PMID: 10082564 Free PMC article.
-
TBP-associated factors are not generally required for transcriptional activation in yeast.Nature. 1996 Sep 12;383(6596):188-91. doi: 10.1038/383188a0. Nature. 1996. PMID: 8774887
-
Mechanisms of transcriptional activation and repression can both involve TFIID.Philos Trans R Soc Lond B Biol Sci. 1996 Apr 29;351(1339):517-26. doi: 10.1098/rstb.1996.0050. Philos Trans R Soc Lond B Biol Sci. 1996. PMID: 8735274 Review.
-
Mediator of transcriptional regulation.Trends Biochem Sci. 1996 Sep;21(9):335-7. doi: 10.1016/s0968-0004(96)10051-7. Trends Biochem Sci. 1996. PMID: 8870496 Review.
Cited by
-
Near-zero linking difference upon transcription factor IID binding to promoter DNA.Mol Cell Biol. 1993 Mar;13(3):1872-5. doi: 10.1128/mcb.13.3.1872-1875.1993. Mol Cell Biol. 1993. PMID: 8382777 Free PMC article.
-
A multisubunit complex containing the SWI1/ADR6, SWI2/SNF2, SWI3, SNF5, and SNF6 gene products isolated from yeast.Proc Natl Acad Sci U S A. 1994 Mar 1;91(5):1950-4. doi: 10.1073/pnas.91.5.1950. Proc Natl Acad Sci U S A. 1994. PMID: 8127913 Free PMC article.
-
Yeast RNA polymerase II transcription in vitro is inhibited in the presence of nucleotide excision repair: complementation of inhibition by Holo-TFIIH and requirement for RAD26.Mol Cell Biol. 1998 May;18(5):2668-76. doi: 10.1128/MCB.18.5.2668. Mol Cell Biol. 1998. PMID: 9566886 Free PMC article.
-
Conserved structural motifs within the N-terminal domain of TFIID tau from Xenopus, mouse and human.Nucleic Acids Res. 1992 Jul 25;20(14):3788. doi: 10.1093/nar/20.14.3788. Nucleic Acids Res. 1992. PMID: 1641350 Free PMC article. No abstract available.
-
A severely defective TATA-binding protein-TFIIB interaction does not preclude transcriptional activation in vivo.Mol Cell Biol. 1997 Mar;17(3):1336-45. doi: 10.1128/MCB.17.3.1336. Mol Cell Biol. 1997. PMID: 9032260 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Molecular Biology Databases