HIV-1 Tat protein promotes formation of more-processive elongation complexes

Robert A Marciniak, Phillip A. Sharp

Research output: Contribution to journalArticle

240 Citations (Scopus)

Abstract

The Tat protein of HIV-1 trans-activates transcription in vitro in a cell-free extract of HeLa nuclei. Quantitative analysis of the efficiency of elongation revealed that a majority of the elongation complexes generated by the HIV-1 promoter were not highly processive and terminated within the first 500 nucleotides. Tat trans-activation of transcription from the HIV-1 promoter resulted from an increase in processive character of the elongation complexes. More specifically, the analysis suggests that there exist two classes of elongation complexes initiating from the HIV promoter: a lessprocessive form and a more-processive form. Addition of purified Tat protein was found to increase the abundance of the more-processive class of elongation complex. The purine nucleoside analog, 5,6-dichloro1-β-D-ribofuranosylbenzimidazole (DRB) inhibits transcription in this reaction by decreasing the efficiency of elongation. Surprisingly, stimulation of transcription elongation by Tat was preferentially inhibited by the addition of DRB.

Original languageEnglish (US)
Pages (from-to)4189-4196
Number of pages8
JournalEMBO Journal
Volume10
Issue number13
StatePublished - 1991
Externally publishedYes

Fingerprint

Human Immunodeficiency Virus tat Gene Products
tat Gene Products
HIV-1
Elongation
Transcription
Purine Nucleosides
Cell Extracts
Transcriptional Activation
Nucleotides
HIV
Chemical activation

Keywords

  • HIV-1
  • RNA binding proteins
  • TAR
  • Tat
  • Transcription elongation

ASJC Scopus subject areas

  • Cell Biology
  • Genetics

Cite this

HIV-1 Tat protein promotes formation of more-processive elongation complexes. / Marciniak, Robert A; Sharp, Phillip A.

In: EMBO Journal, Vol. 10, No. 13, 1991, p. 4189-4196.

Research output: Contribution to journalArticle

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