PARP3 Protein, Human (His, StrepⅡ)

PARP3 protein, a mono-ADP-ribosyltransferase, plays a pivotal role in the cellular response to DNA damage, as highlighted in various studies reported in PubMed. Unlike PARP1 and PARP2, PARP3 specifically mediates mono-ADP-ribosylation, targeting glutamate, aspartate, or lysine residues on select proteins, such as histone H2B, XRCC5, and XRCC6, involved in chromatin architecture and DNA metabolism. This protein is instrumental in DNA repair processes, participating in the detection and signaling pathway triggered by DNA strand breaks. In single-strand break repair, it catalyzes mono-ADP-ribosylation of histone H2B, fostering accurate non-homologous end-joining (NHEJ) in collaboration with the XRCC5-XRCC6 heterodimer. PARP3 also suppresses G-quadruplex structures and is associated with various DNA repair factors, contributing to the cellular response to both exogenous and endogenous DNA damage. Additionally, it acts as a negative regulator of immunoglobulin class switch recombination and is capable of ADP-ribosylating DNA strand break termini, showcasing its multifaceted involvement in genomic maintenance and cellular processes.