Poly(ADP-ribose) polymerase 1 interacts with OAZ and regulates BMP-target genes.

Molecular Cardiology Research Institute, Tufts-New England Medical Center and Department of Biochemistry, Tufts University School of Medicine, Boston, MA 02111, USA.
OAZ is a multi zinc finger protein which interacts with several distinct nuclear proteins including Olf-1/EBF, Smad1, and Smad4 and regulates transcription of various genes. Here we show that poly(ADP-ribose) polymerase 1 (Parp1) forms a complex with OAZ and positively regulates BMP-target genes, Xenopus Vent-2 and mouse Smad6 genes. Both wild type and the mutant forms of Parp1, which is deficient in poly(ADP-ribose) polymerase activity, constitutively interact with OAZ; however, the mutant Parp1 did not activate transcription. These results suggest that poly(ADP-ribose) polymerase activity is essential for the transcriptional activation of Vent-2 and Smad6. These results suggest that Parp1 serves as a transcriptional coactivator of OAZ in BMP-dependent gene regulation.
Mesh Terms:
Animals, Blotting, Western, Bone Morphogenetic Proteins, COS Cells, Chromatin, DNA-Binding Proteins, Enzyme Inhibitors, Gene Expression Regulation, Enzymologic, Homeodomain Proteins, Luciferases, Mice, Mutation, Plasmids, Poly(ADP-ribose) Polymerases, Protein Binding, RNA, Reverse Transcriptase Polymerase Chain Reaction, Smad6 Protein, Trans-Activators, Transcription Factors, Transcriptional Activation, Transfection, Transforming Growth Factor beta, Two-Hybrid System Techniques, Xenopus, Xenopus Proteins
Biochem. Biophys. Res. Commun. Nov. 21, 2003; 311(3);702-7 [PUBMED:14623329]
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