PARP1 Represses PAP and Inhibits Polyadenylation during Heat Shock

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...

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Published in	Molecular cell Vol. 49; no. 1; pp. 7 - 17
Main Authors	Di Giammartino, Dafne Campigli, Shi, Yongsheng, Manley, James L.
Format	Journal Article
Language	English
Published	United States Elsevier Inc 10.01.2013
Subjects	ADP-ribosylation beta-Globins - genetics beta-Globins - metabolism binding capacity Cell Line Enzyme Activation Gene Knockdown Techniques genes heat heat shock proteins Heat-Shock Response Humans inhibition messenger RNA NAD ADP-ribosyltransferase Poly (ADP-Ribose) Polymerase-1 Poly(ADP-ribose) Polymerases - chemistry Poly(ADP-ribose) Polymerases - genetics Poly(ADP-ribose) Polymerases - metabolism Poly(ADP-ribose) Polymerases - physiology Polyadenylation Polynucleotide Adenylyltransferase - chemistry Polynucleotide Adenylyltransferase - metabolism post-translational modification Protein Binding Protein Processing, Post-Translational RNA Interference RNA, Messenger - genetics RNA, Messenger - metabolism thermal stress
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ISSN	1097-2765 1097-4164 1097-4164
DOI	10.1016/j.molcel.2012.11.005

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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. [Display omitted] ► PARP1 binds and PARylates PAP in vitro, which inhibits its polyadenylation activity ► Polyadenylation is inhibited during heat shock in a PARP1-dependent manner ► PAP is PARylated in vivo during heat shock ► Inhibition of polyadenylation reflects decreased RNA binding by PARylated PAP
AbstractList	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 post-translational modifications. Here we show that the enzyme poly(ADP-ribose) polymerase1 (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 both provide direct evidence that PARylation can control processing of mRNA precursors and also identify PARP1 as a regulator of polyadenylation during thermal stress. 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. [Display omitted] ► PARP1 binds and PARylates PAP in vitro, which inhibits its polyadenylation activity ► Polyadenylation is inhibited during heat shock in a PARP1-dependent manner ► PAP is PARylated in vivo during heat shock ► Inhibition of polyadenylation reflects decreased RNA binding by PARylated PAP 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. 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. 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.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. The 3a2 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.
Author	Manley, James L. Di Giammartino, Dafne Campigli Shi, Yongsheng
AuthorAffiliation	1 Department of Biological Sciences, Columbia University, New York, NY, USA
AuthorAffiliation_xml	– name: 1 Department of Biological Sciences, Columbia University, New York, NY, USA
Author_xml	– sequence: 1 givenname: Dafne Campigli surname: Di Giammartino fullname: Di Giammartino, Dafne Campigli organization: Department of Biological Sciences, Columbia University, New York, NY 10027, USA – sequence: 2 givenname: Yongsheng surname: Shi fullname: Shi, Yongsheng organization: Department of Biological Sciences, Columbia University, New York, NY 10027, USA – sequence: 3 givenname: James L. surname: Manley fullname: Manley, James L. email: jlm2@columba.edu organization: Department of Biological Sciences, Columbia University, New York, NY 10027, USA
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/23219533$$D View this record in MEDLINE/PubMed
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Snippet	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... 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... The 3a2 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...
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SubjectTerms	ADP-ribosylation beta-Globins - genetics beta-Globins - metabolism binding capacity Cell Line Enzyme Activation Gene Knockdown Techniques genes heat heat shock proteins Heat-Shock Response Humans inhibition messenger RNA NAD ADP-ribosyltransferase Poly (ADP-Ribose) Polymerase-1 Poly(ADP-ribose) Polymerases - chemistry Poly(ADP-ribose) Polymerases - genetics Poly(ADP-ribose) Polymerases - metabolism Poly(ADP-ribose) Polymerases - physiology Polyadenylation Polynucleotide Adenylyltransferase - chemistry Polynucleotide Adenylyltransferase - metabolism post-translational modification Protein Binding Protein Processing, Post-Translational RNA Interference RNA, Messenger - genetics RNA, Messenger - metabolism thermal stress
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Title	PARP1 Represses PAP and Inhibits Polyadenylation during Heat Shock
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