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Poly(ADP-ribose) polymerase is a B-MYB coactivator
1Department of Molecular Pharmacology and Pathology, Consorzio Mario Negri Sud, S. Maria Imbaro, via Nazionale, 66030 Chieti, Italy.
The Journal of Biological Chemistry
|April 1, 2000
Summary
Poly(ADP-ribose) polymerase (PARP) binds to the B-MYB transcription factor. PARP enhances B-MYB
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- B-MYB is a nuclear transcription factor involved in cell growth, differentiation, and cancer.
- Cellular proteins may modulate B-MYB transcriptional activity through cofactor interactions.
Purpose of the Study:
- To identify proteins interacting with the B-MYB DNA-binding domain.
- To investigate the role of interacting proteins in B-MYB transcriptional activity.
Main Methods:
- Pull-down assays using glutathione S-transferase-B-MYB fusion protein.
- Protein identification via microsequence analysis.
- Immunoprecipitation and transient transfection assays.
Main Results:
- A 110-kDa protein, identified as poly(ADP-ribose) polymerase (PARP), was found to bind B-MYB in HL60 cell nuclei.
- PARP enhanced B-MYB transactivation in transient transfection assays.
- PARP's enzymatic activity was not essential for B-MYB-dependent transactivation.
Conclusions:
- PARP acts as a transcriptional cofactor for B-MYB.
- PARP may influence growth control and cancer through its interaction with B-MYB.