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Originally published In Press as doi:10.1074/jbc.M909345199 on March 29, 2000

J. Biol. Chem., Vol. 275, Issue 22, 16681-16689, June 2, 2000
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Cooperative Interactions between PBX, PREP, and HOX Proteins Modulate the Activity of the alpha 2(V) Collagen (COL5A2) Promoter*

Dmitri PenkovDagger , Shizuko TanakaDagger , Giuliana Di Rocco§, Jens Berthelsen, Francesco Blasi, and Francesco RamirezDagger ||

From the Dagger  Brookdale Center in the Department of Biochemistry and Molecular Biology, Mount Sinai School of Medicine, New York University, New York, New York 10029 and § TIGET and  DIBIT, Universitá Vita-Salute San Raffaele, 20132 Milan, Italy

Cell type-specific expression of the human alpha 2(V) collagen (COL5A2) gene depends on a cis-acting element that consists of two contiguous protein binding sites (FPA and FPB) located between nucleotides -149 and -95, relative to the transcription start site. The present study focused on the characterization of the FPB-bound complex. DNA binding assays and cell transfection experiments revealed that the bipartite core sequence of FPB (5'-ATCAATCA-3') binds the PBX1/2, PREP1, and HOXB1 proteins, and this in turn leads to promoter transactivation. In the presence of all three nuclear factors, cooperative interactions between recombinant PBX1 and PREP1 or PBX1 and HOXB1 result in binding of the heterodimers to FPB in vitro. Similarly, overexpression of different combinations of PBX1, PREP1, and HOXB1 transactivates FPB-driven transcription. In contrast to the composition of the FPB complex purified from COL5A2-positive cells, the FPB complex from COL5A2-negative cells contains PBX2 and PREP1 but lacks PBX1. However, PBX1 exogenously introduced into COL5A2-negative cells cannot stimulate FPB-driven transcription unless co-expressed with PREP1. Within the intrinsic limitations of the experimental model, our results indicate that combinatorial interactions among PBX and PREP or HOX proteins are involved in regulating tissue-specific production of collagen V.

* This work was supported by National Institutes of Health Grants AR-386481 and AR42766, Telethon Italy Grant E485, and by funds from Associazione Italiana Ricerche sul Cancro and the Danish Research Academy (to J. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, Mount Sinai School of Medicine, New York University, One Gustave Levy L. Place, Box 1020, New York, NY 10029. Tel.: 212-241-7984; Fax: 212-722-5999; E-mail: ramirf01@doc.mssm.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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