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Nucleic Acids Research Advance Access published online on May 21, 2009
Nucleic Acids Research, doi:10.1093/nar/gkp307
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© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Gene Regulation, Chromatin and Epigenetics

Ets-1 p51 and p42 isoforms differentially modulate Stromelysin-1 promoter according to induced DNA bend orientation

Gabriel Leprivier1, David Baillat1, Agnès Begue1, Brigitte Hartmann2,* and Marc Aumercier1,*

1CNRS UMR 8161, Institut de Biologie de Lille, Institut Pasteur de Lille, Université de Lille 1 and Lille 2, IFR 142, B.P. 447, 1 rue Calmette, 59021 Lille Cedex and 2LBT, CNRS UPR 9080, 13 rue Pierre et Marie Curie, Paris 75005, France and INSERM UMR S 665, 6 rue Cabanel, 75015 Paris, France

*To whom correspondence should be addressed. Tel: +33 320 871 097; Fax: +33 320 871 111; Email: marc.aumercier{at}ibl.fr Correspondence may also be addressed to Brigitte Hartmann. Tel: +33 143 065 019; Fax: +33 144 493 000; Email: brigitte.hartmann{at}univ-paris-diderot.fr

Received February 13, 2009. Revised April 15, 2009. Accepted April 16, 2009.

The Stromelysin-1 gene promoter contains a palindrome of two Ets-binding sites (EBS) that bind the p51 and p42 isoforms of the human Ets-1-transcription factor. A previous study established that full gene transactivation is associated with a ternary complex consisting of two p51 bound to the two EBS on the promoter. p42, only able to bind one of the two EBS, induces only very weak activity. Here, we investigate the mechanism by which the Stromelysin-1 promoter discriminates between p51 and p42. The differential stoichiometry of the two Ets-1 isoforms arises from the Stromelysin-1 EBS palindrome. The ternary complex requires the presence of two inhibitory domains flanking the DNA-binding domain and the ability to form an intramolecular autoinhibition module. Most importantly, the p51-ternary and the p42-binary complexes induce DNA curvatures with opposite orientations. These results establish that differential DNA bending, via p51 and p42 differential binding, is correlated with the Stromelysin-1 promoter activation process.

Present addresses: Leprivier Gabriel, Department of Molecular Oncology, British Columbia Cancer Research Centre, Vancouver, British Columbia V5Z 1L3, Canada Baillat David, Centro de Regulación Genòmica (CRG), calle Dr. Aiguader, 88, 08003 Barcelona, España


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