Poly(ADP-ribose) polymerase is a B-MYB coactivator.

B-MYB is implicated in cell growth control, differentiation, and cancer and belongs to the MYB family of nuclear transcription factors. Evidence exists that cellular proteins bind directly to B-MYB, and it has been hypothesized that B-MYB transcriptional activity may be modulated by specific cofactors. In an attempt to isolate proteins ...
that interact with the B-MYB DNA-binding domain, a modular domain that has the potential to mediate protein-protein interaction, we performed pull-down experiments with a glutathione S-transferase-B-MYB protein and mammalian protein extracts. We isolated a 110-kDa protein associated endogenously with B-MYB in the nuclei of HL60 cells. Microsequence analysis and immunoprecipitation experiments determined that the bound protein was poly(ADP-ribose) polymerase (PARP). Transient transfection assays showed that PARP enhanced B-MYB transactivation and that PARP enzymatic activity is not required for B-MYB-dependent transactivation. These results suggest that PARP, as a transcriptional cofactor of a potentially oncogenic protein, may play a role in growth control and cancer.
Mesh Terms:
Animals, Binding Sites, Cell Cycle Proteins, Cell Nucleus, DNA-Binding Proteins, Glutathione Transferase, HL-60 Cells, Humans, Mammals, Oncogene Proteins, Osteosarcoma, Poly(ADP-ribose) Polymerases, Protein Biosynthesis, Recombinant Fusion Proteins, Trans-Activators, Transcription, Genetic, Tumor Cells, Cultured
J. Biol. Chem.
Date: Apr. 07, 2000
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