Bovine thymus poly(adenosine diphosphate ribose) polymerase.

Yoshihara, Koichiro; Hashida, T; Tanaka, Yasuharu; Ohgushi, Hajime; Yoshihara, H; Kamiya, Tomoya

doi:10.1016/s0021-9258(19)46955-x

Cited by 100 publications

(33 citation statements)

References 43 publications

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“…(2 mg/mL, in buffer I) with 33 ng/mL plasmin at 25 °C either in the absence or presence of coenzymic DNA (Yoshihara et al, 1978;Niedergang et al, 1979) resulted in complete disappearance of ADPRT activity, inactivation following first-order kinetics (not shown). When the digestion of ADPRT by plasmin was arrested at various time intervals with soybean trypsin inhibitor (20 Mg/mL of digestion mixture) and the quantity of the remaining unhydrolyzed ADPRT protein determined in SDS-PAGE bands (see Experimental Procedures), enzyme inactivation and the rate of disappearance of the ADPRT molecule (Mr 120000) ran exactly parallel.…”

Section: Resultsmentioning

confidence: 94%

“…Coenzymic DNA was obtained as a side product from the ADPRT purification (Buki et al, 1987) and was rendered protein-free by phenol extraction. It consisted mainly of double-stranded DNA of 300 bp on average (Yoshihara et al, 1978;Niedergang et al, 1979). Lysine-Sepbarose 4B was made according to Chibber et al (1974), starting with CNBr-activated Sepharose 4B (Pharmacia).…”

Section: Methodsmentioning

confidence: 99%

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Polypeptide domains of ADP-ribosyltransferase obtained by digestion with plasmin

Büki

Kun²

1988

Biochemistry

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Proteolysis by plasmin inactivates bovine ADP-ribosyltransferase; therefore, enzymatic activity depends exclusively on the intact enzyme molecule. The transferase was hydrolyzed by plasmin to four major polypeptides, which were characterized by affinity chromatography and N-terminal sequencing. Based on the cDNA sequence for human ADP-ribosyltransferase enzyme [Uchida, K., Morita, T., Sato, T., Ogura, T., Yamashita, R., Noguchi, S., Suzuki, H., Nyunoya, H., Miwa, M., & Sugimura, T. (1987) Biochem. Biophys. Res. Commun. 148, 617-622], a polypeptide map of the bovine enzyme was constructed by superposing the experimentally determined N-terminal sequences of the isolated polypeptides on the human sequence deduced from its cDNA. Two polypeptides, the N-terminal peptide (Mr 29,000) and the polypeptide adjacent to it (Mr 36,000), exhibited binding affinities toward DNA, whereas the C-terminal peptide (Mr 56,000), which accounts for the rest of the transferase protein, bound to the benzamide-Sepharose affinity matrix, indicating that it contains the NAD+-binding site. The fourth polypeptide (Mr 42,000) represents the C-terminal end of the larger C-terminal fragment (Mr 56,000) and was formed by a single enzymatic cut by plasmin of the polypeptide of Mr 56,000. The polypeptide of Mr 42,000 still retained the NAD+-binding site. The plasmin-catalyzed cleavage of the polypeptide of Mr 56,000-42,000 was greatly accelerated by the specific ligand NAD+. Out of a total of 96 amino acid residues sequenced here, there were only 6 conservative replacements between human and bovine ADP-ribosyltransferase.

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Section: Resultsmentioning

confidence: 94%

Section: Methodsmentioning

confidence: 99%

Polypeptide domains of ADP-ribosyltransferase obtained by digestion with plasmin

Büki

Kun²

1988

Biochemistry

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“…3-Aminobenzamide (3-AB) and phorbol 12myristate 13-acetate (PMA) were purchased from Sigma Chemical Co. (St. Louis, MO, U.S.A.). Bovine thymus PARP [37], activated DNA [38], and pADPR [39] were prepared as described, respectively.…”

Section: Other Materialsmentioning

confidence: 99%

Evidence for regulation of NF-κB by poly(ADP-ribose) polymerase

Kameoka

Ota

Tetsuka

et al. 2000

Biochemical Journal

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The DNA-binding activity of NF-kappaB in nuclear extracts of poly(ADP-ribose) polymerase (PARP)-defective mutant L1210 cell clones was markedly increased and was inversely correlated with the PARP content in these cells. The DNA-binding activity of NF-kappaB in a clone with the lowest PARP content (Cl-3527, contained 6% of PARP of wild type cells) was about 35-fold of that of the wild-type cells, whereas the change in the DNA-binding activity of AP-1 and SP-1 in the mutant was relatively small or not so significant. Transfection of a PARP-expressing plasmid to the mutant cells decreased the abnormally high levels of NF-kappaB complexes, especially p50/p65(Rel A) complex, to near the normal level. Moreover, poly(ADP-ribosyl)ation of nuclear extracts in vitro suppressed the ability of NF-kappaB to form a complex with its specific DNA probe by approx. 80%. Further analysis with purified recombinant NF-kappaB proteins revealed that both rp50 and rMBP-p65 (Rel A) proteins, but not rGST-IkappaB, could be poly(ADP-ribosyl)ated in vitro and that the modification resulted in a marked decrease in the DNA-binding activity of rMBP-p65, whereas a slight activation was observed in rp50. Poly(ADP-ribosyl)ated p65/NF-kappaB was detected in the cytosol of wild type L1210 cells by immunoblotting with anti-poly(ADP-ribose) and anti-p65 antibodies. Taken together, these results strongly suggest that PARP is involved in the regulation of NF-kappaB through the protein modification.

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“…Isolation of Calf Thymus Poly(ADP-ribose) Polymerase and Coenzymic DNA. Calf thymus poly(ADP-ribose) polymerase was purified to homogeneity, and coenzymic DNA was separated from the enzyme by hydroxylapatite chromatography according to the method of Yoshihara et al (1978). Mono-ADP-ribosylation and poly-ADP-ribosylation were assayed according to Kirsten et al (1985).…”

Section: Methodsmentioning

confidence: 99%

“…Ueda and Hayaishi (1985) and Gaal and Pearson (1985)]. An enzyme-associated DNA species or sequence can be dissociated from the isolated enzyme (Yoshihara et al, 1978) that on a weight basis is more efficient as a "coenzyme" of the polymerase than crude thymus DNA. Several hypotheses were proposed to explain the role of DNA in poly-ADPribosylations.…”

mentioning

confidence: 99%

Covalent binding of 4-carbamoylbenzenediazonium chloride to deoxyguanine bases of DNA resulting in apparent irreversible inhibition of poly(adenosine diphosphoribose) polymerase at the nicotinamide binding site

et al. 1987

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The poly(adenosine diphosphoribose) polymerase activity of isolated liver nuclei was inhibited by 4-carbamoylbenzenediazonium chloride, referred to as 4-diazoniobenzamide, an effect that was dependent on the time of incubation and the concentration of the diazonium compound, with inhibition following first-order kinetics. The inhibition was not reversed by reisolation of nuclei and centrifugal washing, whereas the inhibition by benzamide or 4-aminobenzamide was completely reversible under these conditions. Simultaneous incubation of 4-diazoniobenzamide with benzamide prevented enzyme inhibition. The 4-diazoniobenzoic acid analogue was not inhibitory. The mechanism of action of 4-diazoniobenzamide was traced to a specific covalent binding to dGMP of DNA to form N2-[(4-carbamoylphenyl)azo]-2'-deoxyguanosine 5'-monophosphate. Coenzymic DNA, by tight association with the polymerase protein, fixes the -C(O)NH2 moiety of the adduct at the nicotinamide-binding site of the enzyme.

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Bovine thymus poly(adenosine diphosphate ribose) polymerase.

Cited by 100 publications

References 43 publications

Polypeptide domains of ADP-ribosyltransferase obtained by digestion with plasmin

Polypeptide domains of ADP-ribosyltransferase obtained by digestion with plasmin

Evidence for regulation of NF-κB by poly(ADP-ribose) polymerase

Covalent binding of 4-carbamoylbenzenediazonium chloride to deoxyguanine bases of DNA resulting in apparent irreversible inhibition of poly(adenosine diphosphoribose) polymerase at the nicotinamide binding site

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