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• W2897575728 abstract "Abstract Aberrant transcription-associated RNA:DNA hybrid (R-loop) formation often lead to catastrophic conflicts during replication resulting in DNA double strand breaks and genome instability. To prevent such conflicts, these hybrids require dissolution by helicases and/or RNaseH. Little information is known about how these helicases are regulated. Herein, we identify DDX5, an RGG/RG motif containing DEAD-box family of RNA helicase, as a crucial player in R-loop resolution. We define at the mechanistic level the function of DDX5 in R-loop resolution. In vitro , recombinant DDX5 resolves R-loops in an ATP-dependent manner leading to R-loop degradation by the XRN2 exoribonuclease. DDX5 deficient cells accumulated R-loops at loci known to form R-loops using RNA:DNA immunoprecipitation (DRIP)-qPCR and increased RNaseH sensitive RAD51 foci. PRMT5, an arginine methyltransferase, associated with DDX5 and methylated its RGG/RG motif. This motif was required to associate with XRN2 and resolve cellular R-loops. Furthermore, PRMT5 deficient cells accumulated R-loops, as detected by DRIP-qPCR resulting in increased gH2AX foci. Our findings define a new mechanism by which an RNA helicase, DDX5, is modulated by arginine methylation to resolve R-loops." @default.
• W2897575728 created "2018-10-26" @default.
• W2897575728 creator A5011310066 @default.
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• W2897575728 date "2018-10-24" @default.
• W2897575728 modified "2023-10-18" @default.
• W2897575728 title "Arginine methylation of DDX5 RGG/RG motif by PRMT5 regulates RNA:DNA resolution" @default.
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• W2897575728 doi "https://doi.org/10.1101/451823" @default.
• W2897575728 hasPublicationYear "2018" @default.
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