Direct interaction of human TFIID with the HIV-1 transactivator Tat

Fatah Kashanchi, Graziella Piras, Michael F. Radonovich, Janet F. Duvall, Ali Fattaey, Cheng Ming Chiang, Robert G. Roeder, John N. Brady

Research output: Contribution to journalArticle

209 Citations (Scopus)

Abstract

The tat gene of the human immunodeficiency virus (HIV) plays a central role in the activation and life cycle of HIV. The tat protein (Tat) specifically transactivates HIV transcription in vivo and in vitro1-8, exerting its effects at the level of transcriptional initiation and elongation. Here we report that Tat binds directly to the basal transcription factor TFIID. The transcriptional activity of HeLa extracts was depleted after chromatography on a Tat affinity column, which specifically retained the polymerase H-specific factor TFIID. Direct interaction of Tat with holo-TFIID, composed of TATA-binding protein (TBP) and associated factors (TAFs), was observed. Tat binds, through amino acids 36-50, directly to the TBP subunit of TFIID. Our results suggest that Tat may transduce upstream or downstream regulatory signals by direct interaction with the basal transcription factor TFIID.

Original languageEnglish (US)
Pages (from-to)295-299
Number of pages5
JournalNature
Volume367
Issue number6460
StatePublished - Jan 20 1994

Fingerprint

Transcription Factor TFIID
Trans-Activators
HIV-1
HIV
tat Genes
TATA-Binding Protein Associated Factors
tat Gene Products
TATA-Box Binding Protein
Protein Subunits
Life Cycle Stages
Chromatography
Amino Acids

ASJC Scopus subject areas

  • General

Cite this

Kashanchi, F., Piras, G., Radonovich, M. F., Duvall, J. F., Fattaey, A., Chiang, C. M., ... Brady, J. N. (1994). Direct interaction of human TFIID with the HIV-1 transactivator Tat. Nature, 367(6460), 295-299.

Direct interaction of human TFIID with the HIV-1 transactivator Tat. / Kashanchi, Fatah; Piras, Graziella; Radonovich, Michael F.; Duvall, Janet F.; Fattaey, Ali; Chiang, Cheng Ming; Roeder, Robert G.; Brady, John N.

In: Nature, Vol. 367, No. 6460, 20.01.1994, p. 295-299.

Research output: Contribution to journalArticle

Kashanchi, F, Piras, G, Radonovich, MF, Duvall, JF, Fattaey, A, Chiang, CM, Roeder, RG & Brady, JN 1994, 'Direct interaction of human TFIID with the HIV-1 transactivator Tat', Nature, vol. 367, no. 6460, pp. 295-299.
Kashanchi F, Piras G, Radonovich MF, Duvall JF, Fattaey A, Chiang CM et al. Direct interaction of human TFIID with the HIV-1 transactivator Tat. Nature. 1994 Jan 20;367(6460):295-299.
Kashanchi, Fatah ; Piras, Graziella ; Radonovich, Michael F. ; Duvall, Janet F. ; Fattaey, Ali ; Chiang, Cheng Ming ; Roeder, Robert G. ; Brady, John N. / Direct interaction of human TFIID with the HIV-1 transactivator Tat. In: Nature. 1994 ; Vol. 367, No. 6460. pp. 295-299.
@article{247922f0909b46499d5d9e280b9cfe61,
title = "Direct interaction of human TFIID with the HIV-1 transactivator Tat",
abstract = "The tat gene of the human immunodeficiency virus (HIV) plays a central role in the activation and life cycle of HIV. The tat protein (Tat) specifically transactivates HIV transcription in vivo and in vitro1-8, exerting its effects at the level of transcriptional initiation and elongation. Here we report that Tat binds directly to the basal transcription factor TFIID. The transcriptional activity of HeLa extracts was depleted after chromatography on a Tat affinity column, which specifically retained the polymerase H-specific factor TFIID. Direct interaction of Tat with holo-TFIID, composed of TATA-binding protein (TBP) and associated factors (TAFs), was observed. Tat binds, through amino acids 36-50, directly to the TBP subunit of TFIID. Our results suggest that Tat may transduce upstream or downstream regulatory signals by direct interaction with the basal transcription factor TFIID.",
author = "Fatah Kashanchi and Graziella Piras and Radonovich, {Michael F.} and Duvall, {Janet F.} and Ali Fattaey and Chiang, {Cheng Ming} and Roeder, {Robert G.} and Brady, {John N.}",
year = "1994",
month = "1",
day = "20",
language = "English (US)",
volume = "367",
pages = "295--299",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6460",

}

TY - JOUR

T1 - Direct interaction of human TFIID with the HIV-1 transactivator Tat

AU - Kashanchi, Fatah

AU - Piras, Graziella

AU - Radonovich, Michael F.

AU - Duvall, Janet F.

AU - Fattaey, Ali

AU - Chiang, Cheng Ming

AU - Roeder, Robert G.

AU - Brady, John N.

PY - 1994/1/20

Y1 - 1994/1/20

N2 - The tat gene of the human immunodeficiency virus (HIV) plays a central role in the activation and life cycle of HIV. The tat protein (Tat) specifically transactivates HIV transcription in vivo and in vitro1-8, exerting its effects at the level of transcriptional initiation and elongation. Here we report that Tat binds directly to the basal transcription factor TFIID. The transcriptional activity of HeLa extracts was depleted after chromatography on a Tat affinity column, which specifically retained the polymerase H-specific factor TFIID. Direct interaction of Tat with holo-TFIID, composed of TATA-binding protein (TBP) and associated factors (TAFs), was observed. Tat binds, through amino acids 36-50, directly to the TBP subunit of TFIID. Our results suggest that Tat may transduce upstream or downstream regulatory signals by direct interaction with the basal transcription factor TFIID.

AB - The tat gene of the human immunodeficiency virus (HIV) plays a central role in the activation and life cycle of HIV. The tat protein (Tat) specifically transactivates HIV transcription in vivo and in vitro1-8, exerting its effects at the level of transcriptional initiation and elongation. Here we report that Tat binds directly to the basal transcription factor TFIID. The transcriptional activity of HeLa extracts was depleted after chromatography on a Tat affinity column, which specifically retained the polymerase H-specific factor TFIID. Direct interaction of Tat with holo-TFIID, composed of TATA-binding protein (TBP) and associated factors (TAFs), was observed. Tat binds, through amino acids 36-50, directly to the TBP subunit of TFIID. Our results suggest that Tat may transduce upstream or downstream regulatory signals by direct interaction with the basal transcription factor TFIID.

UR - http://www.scopus.com/inward/record.url?scp=0028181310&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028181310&partnerID=8YFLogxK

M3 - Article

C2 - 8121496

AN - SCOPUS:0028181310

VL - 367

SP - 295

EP - 299

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6460

ER -