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A more recent version of this article appeared on August 9, 2002
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M200088200v1
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Papers In Press, published online ahead of print May 28, 2002
J. Biol. Chem, 10.1074/jbc.M200088200
Submitted on January 4, 2002
Revised on May 28, 2002
Accepted on May 28, 2002

ETS-1 transcription factor binds cooperatively to the palindromic head to head ETS binding sites of the stromelysin-1 promoter by counteracting auto-inhibition

David Baillat, Agnès Bègue, Dominique Stéhelin, and Marc Aumercier

Institut de Biologie de Lille, CNRS UMR 8526, 59021, Lille Cedex

Corresponding Author: marc.aumercier{at}ibl.fr

Stromelysin-1 (MMP-3) is a member of the matrix metalloproteinase family. Regulation of its gene expression is critical for tissue homeostasis. Patterns of increased co-expression of stromelysin-1 and ETS-1 genes have been observed in pathological processes. Stromelysin-1 promoter is transactivated by ETS proteins through two palindromic head to head ETS binding sites (EBS), an unusual configuration among metalloproteinase promoters. Using surface plasmon resonance (SPR), electrophoretic mobility shift assay (EMSA) and photo-crosslinking, we show that full length human ETS-1 (p51) binds cooperatively to the EBS palindrome of the human stromelysin-1 promoter, with facilitated binding of the second ETS-1 molecule to form a ETS-1-DNA-ETS-1 ternary complex. Study of NH2-deletion mutants enables concluding that cooperative binding implies auto-inhibition counteracting, requiring the 245-330 region of the protein which is encoded by Exon VII of the gene. This region is deleted in the natural p42 isoform of ETS-1 which is unable to bind cooperatively to the palindrome. Transient transfection experiments show a good correlation between DNA binding and promoter transactivation for p51. In contrast, p42 shows a poorer transactivation reinforcing the significance of cooperative binding for full transactivation. It is the first time that ETS-1 is shown to be able to counteract its own auto-inhibition.


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