On the biological role of the nuclear polymerizing NAD+: Protein(ADP-ribosyl) transferase (ADPRT): ADPRT from Dictyostelium discoideum and inactivation of the ADPRT gene in the mouse

Auer, Bernhard; Flick, Karin; Wang, Z.Q.; Haidacher, D.; Jäger, Sonja; Berghammer, Heinrich; Kofler, Barbara; Schweiger, Manfred; Wagner, Erwin F.

doi:10.1016/0300-9084(96)88158-2

Cited by 6 publications

(2 citation statements)

References 21 publications

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“…Using the sequence of the catalytic domain of a pADPRT homologue from Dictyostelium [21] for searching the EST databases, we discovered highly similar sequences of both human and mouse origin which we extended by RACE methods to obtain complete cDNAs. The translated pADPRT‐2 sequences were homologous to the C‐terminal catalytic region of pADPRT‐1 enzymes (from aa 485 of mammalian pADPRT‐1, Fig.…”

Section: Resultsmentioning

confidence: 99%

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

et al. 1999

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Until recently, poly(ADP-ribosyl)ation was supposed to be confined only to polymerizing(ADP-ribosyl)transferase/ (ADP-ribose)polymerase (E.C. 2.4.2.30). Here, we present novel polymerizing(ADP-ribosyl)transferase homologues from mouse and man that lack all of the N-terminal DNA binding and BRCA1 C-terminus domains and will be designated polymerizing(ADP-ribosyl)transferase-2 as distinguished from the classical polymerizing(ADP-ribosyl)transferase (polymerizing(ADPribosyl)transferase-1). The murine polymerizing(ADP-ribosyl)-transferase-2 gene shares three identical intron positions with its Caenorhabditis elegans (EMBL nucleotide sequence database Z47075) and one with the Arabidopsis thaliana homologue (`APP', GenBank database AF069298). Expression of the murine polymerizing(ADP-ribosyl)transferase-2 gene was elevated in spleen, thymus and testis and the corresponding poly(ADP-ribosyl)ation activity might account for most of the residual poly(ADP-ribosyl)ation observed in polymerizing(ADPribosyl)transferase-1^/^mice. z 1999 Federation of European Biochemical Societies.

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Section: Resultsmentioning

confidence: 99%

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

et al. 1999

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“…Poly ADPr-polymerase activity was identified in D. discoideum many years ago (Rickwood and Osman, 1979;Kofler et al, 1993;Rajawat et al, 2007;Mir et al, 2015) and a cDNA sequence revealed considerable homology to mammalian PARPs (Auer et al, 1995). The completed genome sequence of D. discoideum (Eichinger et al, 2005) revealed 15 genes encoding proteins with putative ART catalytic domains.…”

Section: Strand Break Repair and Adp-ribosylationmentioning

confidence: 99%

Dictyostelium discoideum as a Model to Assess Genome Stability Through DNA Repair

Pears

Brustel

Lakin

2021

Front. Cell Dev. Biol.

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Preserving genome integrity through repair of DNA damage is critical for human health and defects in these pathways lead to a variety of pathologies, most notably cancer. The social amoeba Dictyostelium discoideum is remarkably resistant to DNA damaging agents and genome analysis reveals it contains orthologs of several DNA repair pathway components otherwise limited to vertebrates. These include the Fanconi Anemia DNA inter-strand crosslink and DNA strand break repair pathways. Loss of function of these not only results in malignancy, but also neurodegeneration, immune-deficiencies and congenital abnormalities. Additionally, D. discoideum displays remarkable conservations of DNA repair factors that are targets in cancer and other therapies, including poly(ADP-ribose) polymerases that are targeted to treat breast and ovarian cancers. This, taken together with the genetic tractability of D. discoideum, make it an attractive model to assess the mechanistic basis of DNA repair to provide novel insights into how these pathways can be targeted to treat a variety of pathologies. Here we describe progress in understanding the mechanisms of DNA repair in D. discoideum, and how these impact on genome stability with implications for understanding development of malignancy.

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Nicotinamide-induced apoptosis in insulin producing cells is associated with cleavage of poly(ADP-ribose) polymerase

Saldeen

Welsh

1998

Molecular and Cellular Endocrinology

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On the biological role of the nuclear polymerizing NAD+: Protein(ADP-ribosyl) transferase (ADPRT): ADPRT from Dictyostelium discoideum and inactivation of the ADPRT gene in the mouse

Cited by 6 publications

References 21 publications

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

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

Dictyostelium discoideum as a Model to Assess Genome Stability Through DNA Repair

Nicotinamide-induced apoptosis in insulin producing cells is associated with cleavage of poly(ADP-ribose) polymerase

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On the biological role of the nuclear polymerizing NAD+: Protein(ADP-ribosyl) transferase (ADPRT): ADPRT from Dictyostelium discoideum and inactivation of the ADPRT gene in the mouse

Cited by 6 publications

References 21 publications

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

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

Dictyostelium discoideum as a Model to Assess Genome Stability Through DNA Repair

Nicotinamide-induced apoptosis in insulin producing cells is associated with cleavage of poly(ADP-ribose) polymerase

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

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