A Class of Activation Domains Interacts Directly with TFIIA and Stimulates TFIIA-TFIID-promoter Complex Assembly

Overview

Journal Mol Cell Biol

Specialty Cell Biology

Date 1995 Nov 1

PMID 7565798

Citations 73

Authors

N Kobayashi

T G Boyer

A J Berk

Affiliations

Soon will be listed here.

Abstract

TFIIA is a general transcription factor that interacts with the TFIID-promoter complex required for transcription initiation by RNA polymerase II. Two lines of evidence suggest that TFIIA is directly involved in the mechanism by which some activators stimulate transcription. First, binding of TFIIA to a TFIID-promoter complex is a rate-limiting step that is enhanced by transcriptional activators GAL4-AH and Zta. Second, recombinant TFIIA greatly enhances activator-dependent transcription. In this study, we found that the activation domains of Zta and VP16 bind directly to TFIIA. Both Zta and VP16 stimulated rapid assembly of a stable TFIID-TFIIA complex on promoter DNA. Analysis of deletion derivatives of the VP16 activation domain indicated that the ability to bind to TFIIA correlates with the ability to enhance TFIID-TFIIA-promoter ternary complex assembly. Thus, we propose that a class of activators stimulate transcription initiation through direct interactions with both TFIIA and TFIID, which stimulate the assembly of an activated TFIIA-TFIID-promoter complex.

Citing Articles

Ino2, activator of yeast phospholipid biosynthetic genes, interacts with basal transcription factors TFIIA and Bdf1.

Engelhardt M, Hintze S, Wendegatz E, Lettow J, Schuller H Curr Genet. 2023; 69(4-6):289-300.

PMID: 37947853 PMC: 10716077. DOI: 10.1007/s00294-023-01277-z.

The Role of VP16 in the Life Cycle of Alphaherpesviruses.

Fan D, Wang M, Cheng A, Jia R, Yang Q, Wu Y Front Microbiol. 2020; 11:1910.

PMID: 33013729 PMC: 7461839. DOI: 10.3389/fmicb.2020.01910.

Distinct requirements of linker DNA and transcriptional activators in promoting SAGA-mediated nucleosome acetylation.

Mittal C, Culbertson S, Shogren-Knaak M J Biol Chem. 2018; 293(35):13736-13749.

PMID: 30054274 PMC: 6120209. DOI: 10.1074/jbc.RA118.004487.

A heterochromatin-dependent transcription machinery drives piRNA expression.

Andersen P, Tirian L, Vunjak M, Brennecke J Nature. 2017; 549(7670):54-59.

PMID: 28847004 PMC: 5590728. DOI: 10.1038/nature23482.

A transcription factor IIA-binding site differentially regulates RNA polymerase II-mediated transcription in a promoter context-dependent manner.

Wang J, Zhao S, He W, Wei Y, Zhang Y, Pegg H J Biol Chem. 2017; 292(28):11873-11885.

PMID: 28539359 PMC: 5512080. DOI: 10.1074/jbc.M116.770412.

References

Horikoshi N, Usheva A, Chen J, Levine A, Weinmann R, Shenk T . Two domains of p53 interact with the TATA-binding protein, and the adenovirus 13S E1A protein disrupts the association, relieving p53-mediated transcriptional repression. Mol Cell Biol. 1995; 15(1):227-34. PMC: 231940. DOI: 10.1128/MCB.15.1.227. View

Thut C, Chen J, Klemm R, Tjian R . p53 transcriptional activation mediated by coactivators TAFII40 and TAFII60. Science. 1995; 267(5194):100-4. DOI: 10.1126/science.7809597. View

Joliot V, Demma M, Prywes R . Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor. Nature. 1995; 373(6515):632-5. DOI: 10.1038/373632a0. View

Sheldon M, Reinberg D . Transcriptional activation. Tuning-up transcription. Curr Biol. 1995; 5(1):43-6. DOI: 10.1016/s0960-9822(95)00014-5. View

Shykind B, Kim J, Sharp P . Activation of the TFIID-TFIIA complex with HMG-2. Genes Dev. 1995; 9(11):1354-65. DOI: 10.1101/gad.9.11.1354. View

Regier J, Shen F, Triezenberg S . Pattern of aromatic and hydrophobic amino acids critical for one of two subdomains of the VP16 transcriptional activator. Proc Natl Acad Sci U S A. 1993; 90(3):883-7. PMC: 45774. DOI: 10.1073/pnas.90.3.883. View

Auble D, Hahn S . An ATP-dependent inhibitor of TBP binding to DNA. Genes Dev. 1993; 7(5):844-56. DOI: 10.1101/gad.7.5.844. View

Liu X, Miller C, Koeffler P, Berk A . The p53 activation domain binds the TATA box-binding polypeptide in Holo-TFIID, and a neighboring p53 domain inhibits transcription. Mol Cell Biol. 1993; 13(6):3291-300. PMC: 359782. DOI: 10.1128/mcb.13.6.3291-3300.1993. View

Manet E, Allera C, Gruffat H, Mikaelian I, Rigolet A, Sergeant A . The acidic activation domain of the Epstein-Barr virus transcription factor R interacts in vitro with both TBP and TFIIB and is cell-specifically potentiated by a proline-rich region. Gene Expr. 1993; 3(1):49-59. PMC: 6081622. View

10.

Roberts S, Ha I, Maldonado E, Reinberg D, Green M . Interaction between an acidic activator and transcription factor TFIIB is required for transcriptional activation. Nature. 1993; 363(6431):741-4. DOI: 10.1038/363741a0. View

11.

Hernandez N . TBP, a universal eukaryotic transcription factor?. Genes Dev. 1993; 7(7B):1291-308. DOI: 10.1101/gad.7.7b.1291. View

12.

Kamakaka R, Bulger M, Kadonaga J . Potentiation of RNA polymerase II transcription by Gal4-VP16 during but not after DNA replication and chromatin assembly. Genes Dev. 1993; 7(9):1779-95. DOI: 10.1101/gad.7.9.1779. View

13.

Boyer T, Berk A . Functional interaction of adenovirus E1A with holo-TFIID. Genes Dev. 1993; 7(9):1810-23. DOI: 10.1101/gad.7.9.1810. View

14.

Merino A, Madden K, Lane W, Champoux J, Reinberg D . DNA topoisomerase I is involved in both repression and activation of transcription. Nature. 1993; 365(6443):227-32. DOI: 10.1038/365227a0. View

15.

Xu X, Prorock C, Ishikawa H, Maldonado E, Ito Y, Gelinas C . Functional interaction of the v-Rel and c-Rel oncoproteins with the TATA-binding protein and association with transcription factor IIB. Mol Cell Biol. 1993; 13(11):6733-41. PMC: 364736. DOI: 10.1128/mcb.13.11.6733-6741.1993. View

16.

Chi T, Carey M . The ZEBRA activation domain: modular organization and mechanism of action. Mol Cell Biol. 1993; 13(11):7045-55. PMC: 364766. DOI: 10.1128/mcb.13.11.7045-7055.1993. View

17.

Baniahmad A, Ha I, Reinberg D, Tsai S, Tsai M, OMalley B . Interaction of human thyroid hormone receptor beta with transcription factor TFIIB may mediate target gene derepression and activation by thyroid hormone. Proc Natl Acad Sci U S A. 1993; 90(19):8832-6. PMC: 47454. DOI: 10.1073/pnas.90.19.8832. View

18.

Wang W, Gralla J, Carey M . The acidic activator GAL4-AH can stimulate polymerase II transcription by promoting assembly of a closed complex requiring TFIID and TFIIA. Genes Dev. 1992; 6(9):1716-27. DOI: 10.1101/gad.6.9.1716. View

19.

Ing N, Beekman J, Tsai S, Tsai M, OMalley B . Members of the steroid hormone receptor superfamily interact with TFIIB (S300-II). J Biol Chem. 1992; 267(25):17617-23. View

20.

Zhou Q, Lieberman P, Boyer T, Berk A . Holo-TFIID supports transcriptional stimulation by diverse activators and from a TATA-less promoter. Genes Dev. 1992; 6(10):1964-74. DOI: 10.1101/gad.6.10.1964. View