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Poly-ADP-ribosylation

McLaren J, Boulikas T, Vamvakas S. 1994. Induction of poly(ADP-ribosyl)ation in the kidney after in vivo application of renal carcinogens. T oxicology 88 101-112. [Pg.278]

Genomic sequence analysis has identified 17 structurally related proteins containing a PARP catalytic domain [3] however, closer inspection suggests that only PARPs 1-3, PARP-4 (vault PARP), and tankyrases 1 and 2 may truly function as poly(ADP-ribosyl)ating proteins. The remaining... [Pg.230]

BRCT BRCAl C-terminus-like DBD DNA-binding domain dPARP Drosophila PARP MPTP l-methyl-4-phenyl-l,2,3,6-tetrahydropyridine NAD+ Nicotinamide adenine dinucleotide NAm Nicotinamide NLS Nuclear locahzation signal OAADPR O-acetyl-ADP-ribose PAR Poly(ADP-ribose) PARG Poly(ADP-ribose) glycohydrolase PARP Poly(ADP-ribose) polymerase PARylation poly(ADP-ribosyl)ation... [Pg.45]

Ame J-C, Jacobson EL, Jacobson MK (2000) ADP-ribose polymer metabolism. In de Murcia G, Shall S (eds) From DNA damage and stress signalhng to cell death poly ADP-ribosylation reactions. Oxford University Press, New York, ppl—34... [Pg.64]

Beneke S, Diefenbach J, Burkle A (2004) Poly(ADP-ribosyl)ation inhibitors promising drug candidates for a wide variety of pathophysiologic conditions. Int J Cancer 111 813-818... [Pg.64]

Burkle A (2001) Physiology and pathophysiology of poly(ADP-ribosyl)ation. Bioessays 23 795-806... [Pg.64]

Curtin NJ (2006) PARP inhibitors and cancer therapy. In Biirlde A (ed) Poly(ADP-Ribosyl)ation. Landes Bioscience, Georgetown, pp218—233... [Pg.65]

Ferro A, Olivera B (1982) Poly(ADP-ribosylation) in vitro. J Biol Chem 257 7808-7813 Gagne JP, Hunter JM, Labrecque B, Chabot B, Poirier GG (2003) A proteomic approach to the identification of heterogeneous nuclear ribonucleoproteins as a new family of poly(ADP-ribose)-binding proteins. Biochem J 371 331-340... [Pg.65]

Krupitza G, Cerutti P (1989) Poly(ADP-ribosylation) of histones in intact human keratinocytes. Biochemistry 28 4054 060... [Pg.66]

Kun E, Kirsten E, Ordahl CP (2002) Coenzymatic activity of randomly broken or intact double-stranded DNAs in auto and histone HI trans-poly(ADP-ribosylation), catalyzed by poly(ADP-ribose) polymerase (PARP I). J Biol Chem 277 39066-39069 Kun E, Kirsten E, Mendeleyev J, Ordahl CP (2004) Regulation of the enzymatic catalysis of poly(ADP-ribose) polymerase by dsDNA, polyamines, Mg2-F, Ca2-F, histones HI and H3, and ATP. Biochemistry 43 210-216... [Pg.66]

Saxena A, Saffery R, Wong L, Kahtsis P, Choo KHA (2002a) Centromere proteins Cenpa, Cenpb, and Bub3 interact with Poly(ADP-ribose) Polymerase-1 protein and are poly(ADP-ribosyl)ated. J Biol... [Pg.68]

A high proportion of the positiveiy charged basic amino acids lysine and arginine within these flexible tails are frequent targets for extensive posttranslational modifications (Berger, 2002). Such modifications include the acetylation of lysine residues, the methylation of lysine and arginine residues, the ubiquitination of lysine residues, the phosphorylation of serine and threonine residues, the sumoylation of lysine residues, and the poly ADP-ribosylation of glutamic acid residues. [Pg.352]

Histone ADP-ribosylation was first reported in 1968 [290]. Poly(ADP-ribosylation) has been implicated in several nuclear processes, including DNA replication, repair and recombination [291-294]. Histone HI and the four core histones are modified by adenosine diphospho (ADP) ribosylation which involves the transfer of the ADP-ribose moiety of NAD" " to the histone acceptor (Figs. 1 and 2). HI is the principle poly(ADP-ribosylated) histone, while core histones are ADP-ribosylated to a minor extent [295-297]. HI is modified at Glu residues 2, 14 (or 15), and 116 (or 117) and at Lys located at the C-terminus [25,298,299]. Poly(ADP-ribosylated) HI is associated with dynamically acetylated core histones [295]. There is conflicting results as to whether poly(ADP-ribosylation) of HI promotes chromatin decondensation [300-304]. [Pg.230]

Realini and Althaus [313] have put forth the hypothesis that poly(ADP-ribosylation) may have a function in histone shuttling. They propose that poly(ADP-ribose) polymerase directed to sites of DNA strand breaks would auto-modify itself generating multiple ADP-ribose polymers. The polymers would lead to the dissociation of the histones from DNA onto the polymers. The DNA would now be free for processing (e.g., by enzymes involved in excision repair). The action of poly(ADP-ribose) glycohydrolase would degrade the... [Pg.230]

Relationships between histone methylation and DNA methylation and histone acetyation and DNA methylation have been reported [191,314,315], A similar relationship may exist between poly(ADP ribosylated) HI and DNA methylation. Inhibition of poly(ADP-ribose) polymerase with 3-aminobenzamide increases the susceptibility of L929 mouse fibroblast nuclei to be methylated by endogenous DNA methyltransferases [316,317], Further, there is evidence that poly(ADP ribosylation) protects CpG islands located at the 5 end of housekeeping genes from methylation [318], Future studies will likely reveal an interesting dynamic relationship between histone methylation, histone acetylation, and histone poly(ADP-ribosylation). [Pg.231]

Fig. 6. Post-translational modifications of core and linker histones. The sites of acetylation, phosphorylation, poly-ADP ribosylation, methylation, and ubiquitination are incficated by numbers that correspond to the amino acid position from the N-termini of the molecules. The nomenclature of histone HI variants is as in Fig. 3. The length of C- and N-terminal tails is in relative scale between core histones to illustrate primary structural differences between these proteins. Fig. 6. Post-translational modifications of core and linker histones. The sites of acetylation, phosphorylation, poly-ADP ribosylation, methylation, and ubiquitination are incficated by numbers that correspond to the amino acid position from the N-termini of the molecules. The nomenclature of histone HI variants is as in Fig. 3. The length of C- and N-terminal tails is in relative scale between core histones to illustrate primary structural differences between these proteins.
Yet another hypothesis considers the somatic variant Hle of histone HI, in its poly(ADP-ribosyl)ated isoform, as a nuclear traw -acting factor involved in maintaining the methylation pattern on DNA [161]. [Pg.333]

Thus, the poly(ADP-ribosyl)ation process is involved in determining and/or maintaining the methylation patterns on DNA. Considering the importance for cells to preserve these patterns, further research will be performed to find additional proof to convalidate one or another mechanism or to identify other possibilities. [Pg.333]

Chromatin fibers from control or poly(ADP-ribosyljated CE nuclei In vitro poly(ADP-ribosyl)ated fibers... [Pg.374]

Poly(ADP-ribosyl)ation induces decondensation of chromatin structure which remains significantly decondensed even in the presence of Mg ions ... [Pg.374]

The major secondary events are changes in membrane structure and permeability, changes in the cytoskeleton, mitochondrial damage, depletion of ATP and other cofactors, changes in Ca2+ concentration, DNA damage and poly ADP-ribosylation, lysosomal destabilization, stimulation of apoptosis, and damage to the endoplasmic reticulum. [Pg.211]

See other pages where Poly-ADP-ribosylation is mentioned: [Pg.138]    [Pg.230]    [Pg.230]    [Pg.46]    [Pg.65]    [Pg.66]    [Pg.66]    [Pg.66]    [Pg.67]    [Pg.67]    [Pg.68]    [Pg.70]    [Pg.70]    [Pg.374]    [Pg.464]    [Pg.309]    [Pg.315]    [Pg.332]    [Pg.332]    [Pg.333]    [Pg.335]    [Pg.380]    [Pg.126]    [Pg.104]   
See also in sourсe #XX -- [ Pg.223 ]

See also in sourсe #XX -- [ Pg.206 ]



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