Nuclear poly (ADPR) and mono (ADPR) residues in tissues with different growth rates

Adamietz, Peter; Bredehorst, Reinhard; Oldekop, M.; Hilz, Helmuth

doi:10.1016/0014-5793(74)80670-8

Cited by 15 publications

(4 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The low capacity in proliferating tissues versus the high activity in resting tissues has been reported (1,6,13,17). The first cell division occurred after 14 to 18 h of germination at 25°C in wheat seeds of this study.…”

supporting

confidence: 50%

Relationship between Poly(Adenosine 5′-diphosphate-ribose) Synthesis and Transcriptional Activity in Wheat Embryo Chromatin

Sasaki

Sugita²

1982

Plant Physiol.

View full text Add to dashboard Cite

Chromatin-bound poly(adenosine 5'-diphosphate IADPI-ribose) synthetase activity was highest in ungerminated wheat ( Triticum aestivum L., cv. Mukakomugi) embryos, and it decreased after germination within 14 hours. In contrast, transcriptional activity was lowest in ungerminated wheat embryos, and it increased during germination for 24 hours or more.Histones, Hi, H2A/H2B, basic nonhistone chromosomal proteins, and acidic nonhistone chromosomal proteins (molecular weight more than 10 kilodaltons) were ADP-ribosylated in wheat germ chromatin. Specific nonhistone chromosomal protein (molecular weight of 37 kilodaltons) in seedling chromatin was not found to be ADP-ribosylated.There are many reports concerning poly(ADP-ribose) synthetase in mammalian cells (5,6,17) but only a few concerning that in plant cells (14,22). In addition to a postulated role in the cell cycle, regulation of DNA repair and replication, gene expression, differentiation, proliferation, and transformation in animal cells (1, 3, 5-7, 11, 13, 15-17, 20); poly(ADP-ribose) may be involved in chromatin condensation (2, 12). Association of poly(ADP-ribose) glycohydrolase with chromatin has been reported in animal (5, 9) and plant (10) After the addition of 5 ml of 5% (w/v) TCA, the acid-insoluble materials were collected on filter paper (Whatman, GF/C) and were washed with 5% (w/v) TCA followed by 95% (v/v) ethanol. After drying, the radioactivity was determined in toluene-based scintillation medium using a Beckman LS 100 liquid scintillation system. In one experiment, [adenylate-32P]

show abstract

supporting

confidence: 50%

Relationship between Poly(Adenosine 5′-diphosphate-ribose) Synthesis and Transcriptional Activity in Wheat Embryo Chromatin

Sasaki

Sugita²

1982

Plant Physiol.

View full text Add to dashboard Cite

show abstract

“…1 A. (A) Control; (B) poly(ADP-ribose) glycohydrolase treatment; (C) phosphodiesterase treatment. 5'-AMP, 3'-AMP, ADP-ribose and adenosine were used as markers presence of polymeric material [30]. The major peak, however, traveled to the position of monomeric ADPribose and a third peak reached the position of 5'-AMP.…”

Section: Fig 2 Chromatographic Analysis Of Histone Hi-bound (Adp-rimentioning

confidence: 99%

ADP-Ribosylated Histone H1 from HeLa Cultures. Fundamental Differences to (ADP-Ribose)n-Histone H1 Conjugates Formed in vitro

1978

View full text Add to dashboard Cite

ADP-ribosylated histone H1 was isolated from intact HeLa cells grown for 24 h with [3H]-adenosine and compared with ADP-ribosylated histone H1 synthesized from [3H]NAD by isolated HeLa nuclei. Most (ADP-ribose),-histone H1 conjugates formed in vivo carried single ADP-ribose units, less than one fourth of the total ADP-ribose residues being in the form of oligomeric or polymeric chains. (ADP-ribose), linked to H1 in vivo was not released by neutral NH2OH to a significant extent. Alkali treatment (pH 10.5) liberated most but not all of the ADP-ribose residues which may indicate the existence of a new type of linkage so far found only in conjugates isolated from intact tissue. No ADP-ribosylated histone H1 complex of higher molecular weight ('HI dimer') could be detected in intact cells.By contrast, isolated HeLa nuclei formed ADP-ribosylated histone H1 which contained predominantly polymeric ADP-ribose residues. The (ADP-ribose), residues were linked by NH20H-sensitive and by NH20H-resistant, alkali (pH 10.5) labile bonds, the majority of the conjugates appearing in the form of the higher-molecular-weight complex.A comparison with the ADP-ribosylated non-histone proteins indicated that histone H1 formed in vivo carried less than 2.5 % of the total protein-bound ADP-ribose residues and less than 1 % of the protein-bound ADP-ribose synthesized in vitro.Poly(ADP-ribose) is formed in cell nuclei by the enzymic transfer of ADP-ribose residues from NAD with the concomitant release of nicotinamide [l -31. Most, if not all (ADP-ribose), residues formed, appear to be linked covalently to nuclear proteins [4,5]. Nishizuka et al. [4] and Otake et al. [5] reported that the histones function as the main acceptor proteins. Others [6,7] showed association of the bulk of protein-bound ADP-ribose residues with the non-histone fraction (for a review see [8,9]), The linkage region of the (ADP-ribose),-protein conjugates is not known. Hayaishi and coworkers postulated an ester glycoside type of linkage because of the high lability of the conjugates formed in vitro towards neutral hydroxylamine and towards alkaline conditions [4]. Supporting evidence for an ester bond involving glutamic acid resi-

show abstract

“…5), indicating phosphorolytic degradation of protein-bound nucleotides by pyrophosphatase (unpublished experiments), known to be present in mitochondria. Incubation with hydroxylamine (18,21,22) at pH 7.4 for 40 min at 25°did not liberate any nucleotides from P protein. When nicotinamide and a freshly prepared mitochondrial extract were incubated simultaneously with the radioactive protein P, besides small amounts of AMP the main product was NAD+, identified by its radioactive labeling and its position on the chromatogram (Fig.…”

mentioning

confidence: 99%

Macromolecular enzymatic product of NAD+ in liver mitochondria.

Kun¹,

Zimber²,

Chang³

et al. 1975

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Rat liver mitochondria contain a Mg2+_ requiring system that transfers the ADP-ribose moiety of NAD+ to an acceptor protein. The enzyme system was extracted in a soluble form and the ADP-ribosylated protein product was isolated by hydroxyapatite and Sephadex chromatography. The ADP-ribosylated protein product has a molecular weight of 100,000 and can be dissociated into subunits of 50,000 daltons by sodium dodecyl sulfate gel electrophoresis. Incubation of the isotopically labeled ADP-ribosylated protein with nicotinamide and a mitochondrial extract yields labeled NAD+, indicating apparent reversibility of the reaction. Enzymatic degradation of the ADP-ribosylated protein with snake venom phosphodiesterase liberates AMP and ADP-ribose or its isomer.Identification of these products and reversibility of the reaction show that the ADP-ribose moiety of NAD+ is the molecular species that is transferred to the acceptor protein. A fraction of the protein-bound ADP-ribose appears to be present as an oligomer. The enzymatic protein-ADPribosylating reaction is inhibited by nicotinamide, ADPribose, the fluorophosphate of AMP, and picrylsulfonic acid.Poly(ADP-ribose) (compare refs. 1-3) and ADP-ribosylated elongation factor 2 (compare refs. 4-6) are presently the only known macromolecular enzymatic products of NAD + in eukaryotic organisms. Both of these NAD+ metabolites exert specific inhibitory effects on cellular macromolecular metabolism of nonmalignant cells. Poly(ADP-ribose) is formed from NAD+ by a chromatin-bound specific polymerase which is dependent on DNA under certain conditions .(compare refs. 2 and 3). The formation of poly(ADP-ribose) coincides with a decreased template activity of isolated chromatin for DNAdirected DNA synthesis in non-malignant cells (7). The exact mechanism of this effect is unknown; however, it was suggested recently that it may be mediated by an inhibition of nuclear endonuclease activity (8). The opposite phenomenon, i.e., activation by poly(ADP-ribose) of apparent template activity is observed in nuclei of HeLa cells (9). ADP-ribosylation of elongation factor 2 by diphtheria toxin, which has a specific ADP-ribose transferase activity from NAD +, is a better understood reversible enzymatic process (4-6). More recently, the peptide structure of the ADP-ribosylated protein has also been described (10).Mitochondria contain specific DNA and it was also shown that these organelles are capable of synthesizing NAD + from nicotinamide and other known precursors (11). It is, therefore, possible that mitochondrial NAD + metabolism could play a hitherto unsuspected cellular regulatory role if macromolecular products of NAD + were found in these subcellular granules. A concrete reason for further investigations along these lines is provided by the discovery of the enzymatic ADPribosylation of a mitochondrial protein by NAD + in extracts of isolated rat liver mitochondria, as described in the present report. METHODS Liver mitochondria were prepared from male albino Wistar rats (130-150 g) s...

show abstract

Nuclear poly (ADPR) and mono (ADPR) residues in tissues with different growth rates

Cited by 15 publications

References 18 publications

Relationship between Poly(Adenosine 5′-diphosphate-ribose) Synthesis and Transcriptional Activity in Wheat Embryo Chromatin

Relationship between Poly(Adenosine 5′-diphosphate-ribose) Synthesis and Transcriptional Activity in Wheat Embryo Chromatin

ADP-Ribosylated Histone H1 from HeLa Cultures. Fundamental Differences to (ADP-Ribose)n-Histone H1 Conjugates Formed in vitro

Macromolecular enzymatic product of NAD+ in liver mitochondria.

Contact Info

Product

Resources

About