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EMBO J. 1991 Dec; 10(13): 4189–4196.
doi: 10.1002/j.1460-2075.1991.tb04997.x
PMCID: PMC453171
PMID: 1756726

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

R A Marciniak and P A Sharp
Author information Copyright and License information PMC Disclaimer

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 less-processive 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-dichloro-1-beta-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.

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Selected References

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