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http://dx.doi.org/10.5483/BMBRep.2020.53.2.264

Methylated-UHRF1 and PARP1 interaction is critical for homologous recombination  

Hahm, Ja Young (Department of Life Science, College of Natural Sciences, Chung-Ang University)
Kang, Joo-Young (Department of Life Science, College of Natural Sciences, Chung-Ang University)
Park, Jin Woo (Department of Life Science, College of Natural Sciences, Chung-Ang University)
Jung, Hyeonsoo (Department of Life Science, College of Natural Sciences, Chung-Ang University)
Seo, Sang-Beom (Department of Life Science, College of Natural Sciences, Chung-Ang University)
Publication Information
BMB Reports / v.53, no.2, 2020 , pp. 112-117 More about this Journal
Abstract
A recent study suggested that methylation of ubiquitin-like with PHD and RING finger domain 1 (UHRF1) is regulated by SET7 and lysine-specific histone demethylase 1A (LSD1) and is essential for homologous recombination (HR). The study demonstrated that SET7-mediated methylation of UHRF1 promotes polyubiquitination of proliferating cell nuclear antigen (PCNA), inducing HR. However, studies on mediators that interact with and recruit UHRF1 to damaged lesions are needed to elucidate the mechanism of UHRF1 methylation-induced HR. Here, we identified that poly [ADP-ribose] polymerase 1 (PARP1) interacts with damage-induced methylated UHRF1 specifically and mediates UHRF1 to induce HR progression. Furthermore, cooperation of UHRF1-PARP1 is essential for cell viability, suggesting the importance of the interaction of UHRF1-PARP1 for damage tolerance in response to damage. Our data revealed that PARP1 mediates the HR mechanism, which is regulated by UHRF1 methylation. The data also indicated the significant role of PARP1 as a mediator of UHRF1 methylation-correlated HR pathway.
Keywords
Homologous recombination; Methylation dependent protein interaction; PARP1; UHRF1;
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