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Volume 272, Number 23, Issue of June 6, 1997 pp. 14883-14892
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

HIV-1 Tat Induces the Expression of the Interleukin-6 (IL6) Gene by Binding to the IL6 Leader RNA and by Interacting with CAAT Enhancer-binding Protein beta  (NF-IL6) Transcription Factors

(Received for publication, November 5, 1996, and in revised form, March 6, 1997)

Concetta Ambrosino Dagger , Maria R. Ruocco Dagger , Xueni Chen § , Massimo Mallardo Dagger , Francesco Baudi Dagger , Sergio Trematerra Dagger , Ileana Quinto Dagger § , Salvatore Venuta Dagger and Giuseppe Scala Dagger §

From the Dagger  Department of Clinical and Experimental Medicine, Medical School, University of Reggio Calabria, 88100 Catanzaro, Italy and the § Department of Biochemistry and Biomedical Technology, Medical School, University "Federico II," Naples 80131, Italy

Human immunodeficiency virus type 1 (HIV-1) infection is associated with severe psoriasis, B cell lymphoma, and Kaposi's sarcoma. A deregulated production of interleukin-6 (IL6) has been implicated in the pathogenesis of these diseases. The molecular mechanisms underlying the abnormal IL6 secretion of HIV-1-infected cells may include transactivation of the IL6 gene by HIV-1. Here we report the molecular mechanisms of Tat activity on the expression of the IL6 gene. By using 5' deletion mutants of pIL6Pr-CAT and using IL6:HIV-1-LTR hybrid constructs where discrete regions of the IL6 promoter replaced the TAR sequence in HIV-1 LTR, we identified a short sequence of the 5'-untranslated region of the IL6 mRNA that is required for Tat to trans-activate the IL6 promoter. This sequence acquires a stem-loop structure and includes a UCU sequence that binds to Tat and is necessary for full trans-activation. In addition, we provide the evidence that Tat can function by enhancing the CAAT enhancer-binding protein (C/EBP) DNA binding activity and is able to complex with in vitro translated C/EBPbeta , which is a major mediator of IL6 promoter function. By using the yeast two-hybrid system and immunoprecipitation, we observed that the interaction of Tat with C/EBP proteins also occurred in vivo. The data are consistent with the possibility that Tat may function on heterologous genes by interacting with RNA structures possibly present in a large number of cellular and viral genes. In addition, Tat may function by protein-protein interactions, leading to the generation of heterodimers with specific transcription factors.


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