Poly(ADP‐ribose) metabolizing enzymes in nuclei and nucleoli of <i>Tetrahymena Pyriformis</i>

Tsopanakis, Christofili; Leer, Johan C.; Nielsen, Ole F.; Gocke, Elmar; Shall, Sydney; Westergaard, Ole

doi:10.1016/0014-5793(78)81125-9

Cited by 22 publications

(5 citation statements)

References 12 publications

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“…The mammalian enzymes have a temperature optimum of approximately 25 "C. In the slime mould Physarum polycephalum, the temperature optimum is reported to be less than 10°C (Brightwell et al, 1975), and in Tetrahymena pyriformis the temperature optimum is approximately 18°C (Tsopanakis et al, 1978). It would seem that the temperature optimum is usually approximately 10 "C less than the temperature at which the organism lives.…”

Section: Discussionmentioning

confidence: 99%

Poly(ADP‐Ribose) Polymerase in Plant Nuclei

Chen

Shall

O'Farrell

1994

European Journal of Biochemistry

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We show that poly(ADP-ribose) polymerase is present in maize, pea and wheat nuclei. We have identified the enzyme product as poly(ADP-ribose) by purification and electrophoresis on a DNA sequencing gel. This reveals a polymer ladder consisting of up to 45 residues. The polymer product from maize, after digestion with snake venom phosphodiesterase, gave only 5'-AMP and (phosphoribosy1)-AMP; the mean chain length of the polymer was 5 and 11 residues in two separate experiments. The optimum pH of the plant enzyme is greater than pH 7.0 in pea, wheat and maize; the optimum temperature for enzyme activity is approximately 15 "C. The K, for NAD' for the enzyme from maize is estimated to be approximately 50 pM under optimal conditions. Several compounds (nicotinamide, deoxythymidine, 3-aminobenzamide, 3-methoxybenzamide and 5-bromodeoxyuridine) that specifically inhibit the animal enzyme also inhibit the enzyme from plants. The ratio of the IC,, for 5-bromodeoxyuridine to the IC,, for 3-aminobenzamide in maize is similar to that of the animal enzyme indicating that the enzyme involved is poly(ADP-ribose) polymerase and not mono(ADP-ribosyl) transferase. SDS gel electrophoresis and gel filtration analysis of a crude extract of maize nuclei indicate a molecular mass for poly(ADP-ribose) polymerase of approximately 114 kDa.

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Section: Discussionmentioning

confidence: 99%

Poly(ADP‐Ribose) Polymerase in Plant Nuclei

Chen

Shall

O'Farrell

1994

European Journal of Biochemistry

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“…In contrast, poly(ADP-ribose) glycohydrolase splits the ribosyl-ribose bond between two ADP-ribose units and produces ADP-ribose [21]. The presence of poly(ADPribose) glycohydrolase activity has becn demonstrated in various normal and tumor animal tissues , as well as in the slime mould Physarum polycephulum [29] and in Tetvahymena pyriJbrn7is [30]. Recently Tanuma et al [28] have reported that the glycohydrolase activity is high in the G I phase of HeLa S3 cells but low during mitosis.…”

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confidence: 99%

Isolation and purification of poly(ADP‐ribose) glycohydrolase from pig thymus

Tavassoli

Shall

1983

European Journal of Biochemistry

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Poly(ADP‐ribose) glycohydrolase has been purified about 12 300‐fold from pig thymus with a recovery of 8.5%. The specific activity of the purified enzyme is 13.8 μmol min−1 mg protein−1. The molecular weight was estimated to be 59000 by gel filtration through Sephadex G‐100 in a non‐denaturing solvent. Analysis of the final preparation by sodium dodecyl sulphate gel electrophoresis reveals two protein bands of molecular weigth, 61 500 and 67 500. The Km value for poly(ADP‐ribose) is estimated to be 1.8 μM monomer units. The enzyme preparation is free from phosphodiesterase, NADase and ADP‐ribosyltransferase activities. The purified enzyme is inhibited by cyclic AMP, ADP‐ribose, naphthylamine, histones H1, H2A, H2B, H3, polylysine, polyarginine, polyornithine and protamine. The inhibition by histone is relieved by an equal mass of DNA. Single‐stranded DNA, poly(A), poly(I) and polyvinyl sulphate were inhibitory, but double‐stranded DNA was not inhibitory.

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“…Apparently this role is universal since similar involvement of ADPRT in the development of a variety of organisms is known (9)(10)(11)(12)(13). The exact role of ADPRT in differentiation is not known, and this role has been projected for the most part from the developmentarresting effects of benzamide-type (1 5 ) nicotinamidebinding site-oriented inhibitors (1) of ADPRT.…”

Section: Discussionmentioning

confidence: 96%

Apparent Role of Adenosine Diphosphoribosyl Transferase in the Development of Mytilus edulis and the Inhibition of Differentiation by Ligands of the Enzyme Protein

Bauer

Kline

Kun

1991

Experimental Biology and Medicine

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The poly(ADP-ribose) polymerase or transferase (ADPRT) activity of developing embryos of Mytilus edulis increases with the progression of larval growth. ADPRT protein was partially purified from 2-hr-old embryos and identified by gel electrophoresis and immunotransblot, demonstrating cross-reactivity with anti-ADPRT IgG produced against the calf thymus enzyme. Two inhibitors of ADPRT, benzamide, competing with NAD at the nicotinamide binding site, and 6-amino-1,2-benzopyrone, which competes with DNA at the DNA binding site(s), both selectively arrest differentiation at the prodissoconch stage. The DNA site-oriented inhibitor, 6-amino-1,2-benzopyrone, has a much larger differentiation arresting effect than benzamide. The arrest of differentiation by 6-amino-1,2-benzopyrone is reversible. A probable ecotoxicity of ADPRT ligands on mussel differentiation is proposed.

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Poly(ADP‐ribose) metabolizing enzymes in nuclei and nucleoli of Tetrahymena Pyriformis

Cited by 22 publications

References 12 publications

Poly(ADP‐Ribose) Polymerase in Plant Nuclei

Poly(ADP‐Ribose) Polymerase in Plant Nuclei

Isolation and purification of poly(ADP‐ribose) glycohydrolase from pig thymus

Apparent Role of Adenosine Diphosphoribosyl Transferase in the Development of Mytilus edulis and the Inhibition of Differentiation by Ligands of the Enzyme Protein

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