Enhanced activity of human G6PD promoter transfected in HeLa cells producing high levels of HIV-1 Tat.

Abstract Glucose 6-phoshate dehydrogenase (G6PD) enzyme activity has an important role in the cell defence against oxidative damage produced by hydrogen peroxide, a compound known to activate HIV-1 expression through the intermediate of NF-κB. By means of CAT assays, in this paper we show that the Tat protein increases the rate of transcription from the human G6PD promoter in HeLa cells; furthermore, we report a similar effect of Tat on transcription driven from the viral RSV promoter. We did not observe Tat stimulation with the human CMV, SV40 or the basic RSV promoters. Dose-response curves indicate that Tat activates G6PD and RSV through a mechanism different from the major one operating on the HIV-1 LTR promoter. TAR-like structures are not involved, instead a short sequence close to the G6PD transcription start site and the RSV LTR enhancer is a good candidate for mediating the phenomena described in this paper. This sequence has some features in common with the NF-κB motif.