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  • 1
    Electronic Resource
    Electronic Resource
    Comparison of the ADP-ribosylating thermozyme from Sulfolobus solfataricus and the mesophilic poly(ADP-ribose) polymerases (2000)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 192 (2000), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The poly(ADP-ribose) polymerase-like thermozyme purified from Sulfolobus solfataricus was characterised with respect to some physico-chemical properties. The archaeal protein exhibited a scarce electrophoretic mobility at both pH 2.9 and pH 7.5. Determination of the isoelectric point (pI=7.0–7.2) allowed us to understand the reason for the limited migration at pH 7.5, while amino acid composition analysis showed a moderate content of basic residues, which reduced mobility at pH 2.9. With respect to the charge, the archaeal enzyme behaved differently from the eukaryotic thermolabile poly(ADP-ribose) polymerase, described as a basic protein (pI=9.5). Well known inhibitors of the mesophilic polymerase like Zn2+, nicotinamide and 3-aminobenzamide exerted a smaller effect on the enzyme from S. solfataricus, reducing the activity by at most 50%. Mg2+ was a positive effector, although in a dose-dependent manner. It influenced the fluorescence spectrum of the archaeal protein, whereas NaCl had no effect.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2000.tb09351.x
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  • 2
    Electronic Resource
    Electronic Resource
    In vitro inhibition of HeLa cell nuclear ribonucleases by ADP-ribosylation (1990)
    Springer
    Molecular and cellular biochemistry 94 (1990), S. 53-60 
    Details
    ISSN: 1573-4919
    Keywords: nuclear ribonucleases ; poly(ADP-ribose)polymerase (HeLa Cell)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Ribonuclease activity in HeLa cell nuclei is markedly inhibited by ADP-ribosylation following incubation of intact isolated nuclei with [14C]NAD. Time course experiments demonstrate that [24C] incorporation into proteins is accompanied by a 50% inhibition of ribonuclease activity on single-strand and double-strand polynucleotides. Inhibition does not occur when 3-aminobenzamide, a potent (ADP-ribose)polymerase inhibitor, is present. Two enzymatic activities that degrade double-strand polynucleotides have been purified and partially characterized. A relevant level of radioactivity resulting from [14C]NAD incubation of nuclei was associated to the purified enzyme. The RNase Fl component, which shows maximal activity on polyU-polyA is demonstrated to be the major ADP-ribose acceptor protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00223562
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  • 3
    Electronic Resource
    Electronic Resource
    The analysis of the poly(ADPR)polymerase mode of action in rat testis nuclear fractions defines a specific poly(ADP-ribosyl)ation system associated with the nuclear matrix (2000)
    Springer
    Molecular and cellular biochemistry 205 (2000), S. 91-99 
    Details
    ISSN: 1573-4919
    Keywords: poly(ADPR)polymerase ; histone proteins ; chromatin structure ; nuclear matrix
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The poly(ADP-ribosyl)ation system, associated with different nuclear fractions of rat testis, has been analyzed for both pADPR and pADPR acceptor proteins. The DNase I sensitive and resistant chromatin contain 35% and 40%, respectively, of the total pADPR synthesized in intact nuclei incubated with [32P]NAD. Moreover, the residual 25% were estimated to be associated with the nuclear matrix.Three different classes of pADPR are present in the nuclei. The longest and branched ADPribose polymers modify proteins present in the DNase I resistant (2 M NaCl extractable) chromatin and in the nuclear matrix, whereas polymers of 〉 20 residues interact with the components of the DNase I sensitive chromatin and oligomers of 6 ADPribose residues are bound specifically to the acid-soluble chromosomal proteins, present in isolated nuclear matrix. The main pADPR acceptor protein in all the nuclear fractions is represented by the PARP itself (auto-modification reaction). The hetero-modification reaction occurs mostly on histone H1 and core histones, that have been found associated to DNase I sensitive and resistant chromatin, respectively. Moreover, an oligo(ADP-ribosyl)ation occurs on core histones tightly-bound to the matrix associated regions (MARs) of chromatin loops.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007005715848
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  • 4
    Electronic Resource
    Electronic Resource
    Inhibition of ADP-ribosylation of histone H1 by analogs of diadenosine 5′, 5‴-p1,p4-tetraphosphate (1987)
    Springer
    Molecular and cellular biochemistry 74 (1987), S. 17-20 
    Details
    ISSN: 1573-4919
    Keywords: ADP-ribosylation ; diadenosine 5′,5‴-p1,p4-tetraphosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The effects of analogs of diadenosine 5′,5‴-p1,p4-tetraphosphate (Ap4A) were examined on the ADP-ribosylation reaction of histone Hl catalysed by purified bovine thymus poly(ADP-ribose)transferase. Among the compounds tested, εAp4A and ApCH2PPPA were shown to be the most efficient inhibitors of the enzyme. From kinetic studies of their action, it appears that εAp4A and ApCH2pppA might be ‘mixed type’ inhibitors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00221908
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  • 5
    Electronic Resource
    Electronic Resource
    Poly(ADPribosyl)ation system in transcriptionally active rat testis chromatin fractions (1996)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 63 (1996), S. 334-341 
    Details
    ISSN: 0730-2312
    Keywords: testis ; transcription ; poly(ADPribose) ; poly(ADPR)polymerase ; DNA repair ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The rat testis chromatin fractions (soluble, S, and insoluble, P) were prepared by mild digestion of nuclei with DNAase I. They appeared to be different in specific biochemical features such as their transcriptional competence and protein patterns, the latter indicating, according to results previously obtained, that the testis-specific H1t is preferentially associated to the soluble fraction, whereas the other H1 variants are localized in the pellet. S and P chromatins also differed in the distribution of the poly(ADP-ribosyl)ating system, (poly(ADP-ribose)polymerase, reaction product and acceptor proteins), detected by incubating nuclei with 32P-NAD. The 32P-modified H1s and core histones of both fractions, known as specific ADPribose target proteins, were separated by high performance liquid chromatography and it was demonstrated that the H1 variants from S and P are differently ADPribosylated, being H1t always the best acceptor, and that most of the ADPribosylated variants were solubilized after DNase I treatment. The further digestion of P chromatin with the nuclease produced a fraction (pP) devoid of most DNA, but particularly enriched in transcriptionally competent tracts. The low DNA content of pP chromatin, which reflects the typical feature of a nuclear matrix, corresponded to a relevant poly(ADPribosyl)ation, the highest as compared to S and P fractions. Moreover, long and branched chains of poly(ADP-ribose) were found associated to pP sample which resemble the products determined in the soluble chromatin. © 1996 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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