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Molecular and Cellular Biology, April 1999, p. 2803-2816, Vol. 19, No. 4
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Specific Binding of High-Mobility-Group I (HMGI) Protein and Histone H1 to the Upstream AT-Rich Region of the Murine Beta Interferon Promoter: HMGI Protein Acts as a Potential Antirepressor of the Promoter

Eliette Bonnefoy,* Marie-Thérèse Bandu, and Janine Doly

Laboratoire de Régulation de l'Expression des Gènes Eucaryotes, CNRS, UPR37, UFR Biomédicale, Université René Descartes, 75270 Paris Cedex 06, France

Received 25 June 1998/Returned for modification 17 August 1998/Accepted 11 January 1999

The high-mobility-group I (HMGI) protein is a nonhistone component of active chromatin. In this work, we demonstrate that HMGI protein specifically binds to the AT-rich region of the murine beta interferon (IFN-beta ) promoter localized upstream of the murine virus-responsive element (VRE). Contrary to what has been described for the human promoter, HMGI protein did not specifically bind to the VRE of the murine IFN-beta promoter. Stably transfected promoters carrying mutations on this HMGI binding site displayed delayed virus-induced kinetics of transcription. When integrated into chromatin, the mutated promoter remained repressed and never reached normal transcriptional activity. Such a phenomenon was not observed with transiently transfected promoters upon which chromatin was only partially reconstituted. Using UV footprinting, we show that the upstream AT-rich sequences of the murine IFN-beta promoter constitute a preferential binding region for histone H1. Transfection with a plasmid carrying scaffold attachment regions as well as incubation with distamycin led to the derepression of the IFN-beta promoter stably integrated into chromatin. In vitro, HMGI protein was able to displace histone H1 from the upstream AT-rich region of the wild-type promoter but not from the promoter carrying mutations on the upstream high-affinity HMGI binding site. Our results suggest that the binding of histone H1 to the upstream AT-rich region of the promoter might be partly responsible for the constitutive repression of the promoter. The displacement by HMGI protein of histone H1 could help to convert the IFN-beta promoter from a repressed to an active state.

* Corresponding author. Mailing address: Laboratoire de Régulation de l'Expression des Gènes Eucaryotes, CNRS, UPR37, UFR Biomédicale, Université René Descartes, 45 rue des Saints-Pères, 75270 Paris Cedex 06, France. Phone: (33) 01.42.86.22.76. Fax: (33) 01.42.62.55.37. E-mail: bonnefoy{at}biomedicale.univ-paris5.fr.

Molecular and Cellular Biology, April 1999, p. 2803-2816, Vol. 19, No. 4
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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