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• W2023788813 abstract "The 3' ends of most eukaryotic mRNAs are produced by an endonucleolytic cleavage followed by synthesis of a poly(A) tail. Poly(A) polymerase (PAP), the enzyme that catalyzes the formation of the tail, is subject to tight regulation involving several posttranslational modifications. Here we show that the enzyme poly(ADP-ribose) polymerase 1 (PARP1) modifies PAP and regulates its activity both in vitro and in vivo. PARP1 binds to and modifies PAP by poly(ADP-ribosyl)ation (PARylation) in vitro, which inhibits PAP activity. In vivo we show that PAP is PARylated during heat shock, leading to inhibition of polyadenylation in a PARP1-dependent manner. The observed inhibition reflects reduced RNA binding affinity of PARylated PAP in vitro and decreased PAP association with non-heat shock protein-encoding genes in vivo. Our results provide direct evidence that PARylation can control processing of mRNA precursors, and also identify PARP1 as a regulator of polyadenylation during thermal stress." @default.
• W2023788813 created "2016-06-24" @default.
• W2023788813 creator A5046588710 @default.
• W2023788813 creator A5058898427 @default.
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• W2023788813 date "2013-01-01" @default.
• W2023788813 modified "2023-10-14" @default.
• W2023788813 title "PARP1 Represses PAP and Inhibits Polyadenylation during Heat Shock" @default.
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• W2023788813 doi "https://doi.org/10.1016/j.molcel.2012.11.005" @default.
• W2023788813 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3545032" @default.
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