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Journal of Virology, November 2000, p. 10523-10534, Vol. 74, No. 22
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

High-Mobility-Group Protein I Can Modulate Binding of Transcription Factors to the U5 Region of the Human Immunodeficiency Virus Type 1 Proviral Promoter

Angus Henderson,1 Michael Bunce,1 Nicole Siddon,1 Raymond Reeves,2 and David John Tremethick1,*

The John Curtin School of Medical Research, the Australian National University, Canberra, Australian Capital Territory 2601, Australia,1 and Department of Biochemistry and Biophysics, Washington State University, Pullman, Washington 991642

Received 23 March 2000/Accepted 4 August 2000

HMG I/Y appears to be a multifunctional protein that relies on in its ability to interact with DNA in a structure-specific manner and with DNA, binding transcriptional activators via distinct protein-protein interaction surfaces. To investigate the hypothesis that HMG I/Y may have a role in human immunodeficiency virus type 1 (HIV-1) expression, we have analyzed whether HMG I/Y interacts with the 5' long terminal repeat and whether this interaction can modulate transcription factor binding. Using purified recombinant HMG I, we have identified several high-affinity binding sites which overlap important transcription factor binding sites. One of these HMG I binding sites coincides with an important binding site for AP-1 located downstream of the transcriptional start site, in the 5' untranslated region at the boundary of a positioned nucleosome. HMG I binding to this composite site inhibits the binding of recombinant AP-1. Consistent with this observation, using nuclear extracts prepared from Jurkat T cells, we show that HMG I (but not HMG Y) is strongly induced upon phorbol myristate acetate stimulation and this induced HMG I appears to both selectively inhibit the binding of basal DNA-binding proteins and enhance the binding of an inducible AP-1 transcription factor to this AP-1 binding site. We also report the novel finding that a component present in this inducible AP-1 complex is ATF-3. Taken together, these results argue that HMG I may play a fundamental role in HIV-1 expression by determining the nature of transcription factor-promoter interactions.

* Corresponding author. Mailing address: The John Curtin School of Medical Research, the Australian National University, P.O. Box 334, Canberra, Australian Capital Territory 2601, Australia. Phone: 61-6-249 2326. Fax: 61-6-249 0415. E-mail: David.Tremethick{at}anu.edu.au.

Journal of Virology, November 2000, p. 10523-10534, Vol. 74, No. 22
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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