NOVEL INSIGHTS INTO POLY(ADP-RIBOSE) POLYMERASE 2: A ZINC-DEPENDENT ENZYME AND NUCLEOSOME REMODELER

• Dr. Nadia M. Suleiman

  Department of Molecular Genetics, King Saud University, Saudi Arabia

  Author

• Dr. Tomas H. Eriksson

  Department of Biochemistry and Structural Biology, Lund University, Sweden

  Author

• Dr. Anna M. Kowalska

  Faculty of Biology, University of Warsaw, Poland

  Author

Poly(ADP-ribose) polymerase 2 (PARP2) is a crucial enzyme involved in DNA damage repair and various cellular processes. While extensively studied for its role in base excision repair (BER) in conjunction with PARP1, its inherent characteristics as a metalloenzyme and its direct impact on chromatin structure remain less explored. This article delves into recent findings demonstrating PARP2's zinc-dependent nature, highlighting the significance of zinc ions for its enzymatic activity and structural integrity. Furthermore, it presents evidence for PARP2's direct role in nucleosome reorganization, suggesting a broader involvement in chromatin dynamics beyond its established DNA repair functions. Understanding these novel aspects of PARP2 can pave the way for developing more targeted therapeutic strategies, particularly in cancer treatment where PARP inhibitors are widely used.

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