Interaction of human immunodeficiency virus type 1 Tat with a unique site of TFIID inhibits negative cofactor Dr1 and stabilizes the TFIID-TFIIA complex

Fatah Kashanchi, Samir N. Khleif, Janet F. Duvall, M. Reza Sadaie, Michael F. Radonovich, Michael Cho, Malcolm A. Martin, Sei Yu Chen, Roberto Weinmann, John N. Brady

Research output: Contribution to journalArticle

31 Scopus citations

Abstract

We have previously reported the direct physical interaction between the human immunodeficiency virus (HIV) type 1 Tat protein and the basal transcription factor TBP/TFIID. Affinity chromatography demonstrated that wild-type Tat, but not a transactivation mutant of Tat, was capable of depleting TBP/TFIID from cell extracts. These experiments represented the first demonstration of a basal transcription factor that binds, in an activation-dependent manner, to Tat. We now report that the Tat-TBP interaction can be detected in HIV type 1-infected cells. The domain of TBP interacting with Tat has been mapped from amino acids 163 to 196 by using deletion and site-specific mutants of TBP. This domain of TBP, which includes the H1 and S2 domains, is distinct from the H2 binding site for other activator proteins, such as E1A. The interaction of Tat with TFIID regulates the binding of accessory proteins to TFIID. Tat stabilizes the interaction of TFIID with TFIIA in a gel shift assay. In addition, Tat competes for Dr1 interaction with TBP. Our results suggest that the basal transcription factor TBP/TFIID represents an important regulatory molecule in HIV transcription.

Original languageEnglish (US)
Pages (from-to)5503-5510
Number of pages8
JournalJournal of Virology
Volume70
Issue number8
StatePublished - Aug 1 1996

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

Fingerprint Dive into the research topics of 'Interaction of human immunodeficiency virus type 1 Tat with a unique site of TFIID inhibits negative cofactor Dr1 and stabilizes the TFIID-TFIIA complex'. Together they form a unique fingerprint.

  • Cite this

    Kashanchi, F., Khleif, S. N., Duvall, J. F., Sadaie, M. R., Radonovich, M. F., Cho, M., Martin, M. A., Chen, S. Y., Weinmann, R., & Brady, J. N. (1996). Interaction of human immunodeficiency virus type 1 Tat with a unique site of TFIID inhibits negative cofactor Dr1 and stabilizes the TFIID-TFIIA complex. Journal of Virology, 70(8), 5503-5510.