pADPRT‐2: a novel mammalian polymerizing(ADP‐ribosyl)transferase gene related to truncated pADPRT homologues in plants and <i>Caenorhabditis elegans</i><sup>1</sup>

Berghammer, Heinrich; Ebner, Maria; Marksteiner, Rainer; Auer, Bernhard

doi:10.1016/s0014-5793(99)00448-2

Cited by 52 publications

(39 citation statements)

References 22 publications

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“…The position of the initiation region was close to the most 5Ј-extending mouse and human PARP-2 cDNA originally isolated (6). This confirmed the size of the protein we described (6) as opposed to the shorter form of PARP-2 identified by Berghammer et al (23) and Johansson (9).…”

Section: Organization Of the Parp-2 Gene Vis à Vis The Protein Modules-supporting

confidence: 87%

“…No expression of the GFP reporter was noticed in the absence of the TATA sequence and when the plasmid contained only the intergenic region in addition to the intronic sequence. These results showed that the first intron did not contain any important transcriptional elements nor any other initiation sites as was suggested previously (23).…”

Section: Fig 2 Parp-2 and H1supporting

confidence: 87%

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A Bidirectional Promoter Connects the Poly(ADP-ribose) Polymerase 2 (PARP-2) Gene to the Gene for RNase P RNA

Amé

Schreiber

Fraulob

et al. 2001

Journal of Biological Chemistry

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Poly(ADP-ribose) polymerase 2 (PARP-2) is a DNA damage-dependent enzyme that belongs to a growing family of enzymes seemingly involved in genome protection. To gain insight into the physiological role of PARP-2 and to investigate mechanisms of PARP-2 gene regulation, we cloned and characterized the murine PARP-2 gene. The PARP-2 gene consists of 16 exons and 15 introns spanning about 13 kilobase pairs. Interestingly, the PARP-2 gene lies head to head with the gene encoding the mouse RNase P RNA subunit. The distance between the transcription start sites of the PARP-2 and RNase P RNA genes is 114 base pairs. This suggested that regulation of the expression of both genes may be coordinated through a bi-directional promoter. The PARP-2/RNase P RNA gene organization is conserved in the human. To our knowledge, this is the first report of a RNA polymerase II gene and an RNA polymerase III gene sharing the same promoter region and potentially the same transcriptional control elements. Reporter gene constructs showed that the 113-base pair intergenic region was indeed sufficient for the expression of both genes and revealed the importance of both the TATA and the DSE/Oct-1 expression control elements for the PARP-2 gene transcription. The expression of both genes is clearly independently regulated. PARP-2 is expressed only in certain tissues, and RNase P RNA is expressed in all tissues. This suggests that both genes may be subjected to multiple levels of control and may be regulated by different factors in different cellular contexts.Poly(ADP-ribosylation) is an immediate post-translational modification of nuclear proteins induced by DNA-damaging agents. At a site of breakage, the enzyme poly(ADP-ribose) polymerase 1 (PARP-1, 1 113 kDa) catalyzes the transfer of the ADP-ribose moiety from the respiratory coenzyme NAD ϩ to a limited number of protein acceptors involved in chromatin architecture (histones H1, H2B, lamin B, and high mobility group [HMG] proteins) or in DNA metabolism (DNA replication factors, topoisomerases including PARP-1) (1-3). Auto-and heteromodification of these proteins are part of an obligatory step of a detection/signaling pathway leading ultimately to the resolution of strand interruptions. A variety of molecular and genetic approaches have been developed this last decade that define unambiguously a critical role of PARP-1 in the cell response to DNA damage and repair and in cell death during the inflammatory process (for review, see Shall and de Murcia (4, 5)).Although it was assumed for many years that PARP activity was associated with a single protein (now termed PARP-1) displaying unique DNA damage detection properties, the recent discovery of four members of the PARP family has emphasized an unexpected complexity of poly(ADP-ribosylation) reactions in mammalian cells. We have recently cloned the cDNAs encoding human and murine PARP-2 (62 kDa), which catalyzes the formation of ADP-ribose polymers in a DNA damage-dependent manner (6). Of the three other PARP homologues that have been cloned, ...

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Section: Organization Of the Parp-2 Gene Vis à Vis The Protein Modules-supporting

confidence: 87%

Section: Fig 2 Parp-2 and H1supporting

confidence: 87%

A Bidirectional Promoter Connects the Poly(ADP-ribose) Polymerase 2 (PARP-2) Gene to the Gene for RNase P RNA

Amé

Schreiber

Fraulob

et al. 2001

Journal of Biological Chemistry

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“…In support of these previous findings, in the present study, we show that in wildtype fibroblasts total PARP activation is a very early event, because the enzyme was activated within 15 min after oxidative or immunological challenge. Although PARP-1-deficient cells possess other enzymes capable of some poly(ADP-ribosylation) (13)(14)(15)(16)(17)(18), we found that the catalytic activity was maximally expressed in wild-type cells only. This suggests that, among the PARP homologous enzymes, PARP-1 is the major active enzyme to modulate poly(ADP-ribosylation) and the events leading to DNA repair.…”

Section: Discussionmentioning

confidence: 81%

Poly(ADP-Ribose) Polymerase-1 Regulates Activation of Activator Protein-1 in Murine Fibroblasts

Andreone

O’Connor

Denenberg

et al. 2003

The Journal of Immunology

102

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Poly(ADP-ribose) polymerase (PARP)-1 is activated in response to DNA injury in the nucleus of eukaryotic cells and has been implicated in cell dysfunction in inflammation. We investigated the role of PARP-1 on the AP-1 pathway, which is involved in the signal transduction of the inflammatory process. In murine wild-type fibroblasts, oxidative challenge by peroxynitrite and hydrogen peroxide or immunological challenge by IL-1 and 20% FCS induced phosphorylation of the mitogen-activated protein kinase kinase-4, activation of c-Jun N-terminal kinase (JNK), and DNA binding of AP-1. In comparative experiments, peroxynitrite induced DNA binding of heat shock factor-1. Pretreatment of wild-type cells with 5-iodo-6-amino-1,2-benzopyrone, a PARP-1 inhibitor, inhibited JNK activation and DNA binding of AP-1. In parallel experiments in PARP-1-deficient fibroblasts, DNA binding of AP-1 was completely abolished. Activation of JNK was significantly elevated at basal condition, but it exhibited a lesser increase after oxidative or immunological challenge than in wild-type fibroblasts. Nuclear content of phosphorylated mitogen-activated protein kinase kinase-4 was observed in PARP-1-deficient cells after peroxynitrite challenge only. Western blotting analysis for AP-1 subunits indicated that c-Fos was similarly expressed in wild-type and PARP-1-deficient cells. Phosphorylated c-Jun was expressed after oxidative or immunological challenge, but not in basal condition, in wild-type cells; however, it was significantly elevated at basal condition and further enhanced after oxidative or immunological challenge in PARP-1-deficient cells. No DNA binding of heat shock factor-1 was observed in PARP-1-deficient cells. These data demonstrate that PARP-1 plays a pivotal role in the modulation of transcription.

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“…In vitro, tankyrase catalyzes its automodification as well as the modification of the telomere-specific protein TRF1 in a DNAindependent manner. The third member of the PARP family, PARP-2, is a 62-kDa protein (6,7). It is activated by DNA strand breaks, but its function is unknown.…”

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confidence: 99%

Poly(ADP-ribose) Binds to Specific Domains in DNA Damage Checkpoint Proteins

Pleschke

Kleczkowska²,

Strohm

et al. 2000

Journal of Biological Chemistry

485

457

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pADPRT‐2: a novel mammalian polymerizing(ADP‐ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans¹

Cited by 52 publications

References 22 publications

A Bidirectional Promoter Connects the Poly(ADP-ribose) Polymerase 2 (PARP-2) Gene to the Gene for RNase P RNA

A Bidirectional Promoter Connects the Poly(ADP-ribose) Polymerase 2 (PARP-2) Gene to the Gene for RNase P RNA

Poly(ADP-Ribose) Polymerase-1 Regulates Activation of Activator Protein-1 in Murine Fibroblasts

Poly(ADP-ribose) Binds to Specific Domains in DNA Damage Checkpoint Proteins

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pADPRT‐2: a novel mammalian polymerizing(ADP‐ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans1

Cited by 52 publications

References 22 publications

A Bidirectional Promoter Connects the Poly(ADP-ribose) Polymerase 2 (PARP-2) Gene to the Gene for RNase P RNA

A Bidirectional Promoter Connects the Poly(ADP-ribose) Polymerase 2 (PARP-2) Gene to the Gene for RNase P RNA

Poly(ADP-Ribose) Polymerase-1 Regulates Activation of Activator Protein-1 in Murine Fibroblasts

Poly(ADP-ribose) Binds to Specific Domains in DNA Damage Checkpoint Proteins

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pADPRT‐2: a novel mammalian polymerizing(ADP‐ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans¹