Cellular regulation of ADP-ribosylation of proteins

Sooki-Toth, A.; Bánfalvi, Gáspár; Szöllősi, János; Kirsten, Eva; Staub, Maria; Antoni, Ferenc András; Kun, Ernest

doi:10.1016/0014-4827(89)90362-5

Cited by 10 publications

(1 citation statement)

References 36 publications

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“…However, the low rate of poly(ADP-ribosyl)ation that occurs under physiological conditions and may be correlated to DNA replication may have additional and possibly important self-regulatory functions. For example, the ADP-ribosylation of histone H3 in stimulated cells (Sooki-Toth et al, 1989) may be a specific de-repressing signal to the genome by counteracting the known repressor role of the histone. The second known enzymic function of ADPRT, which is NAD+ glycohydrolase activity (cf.…”

Section: Discussionmentioning

confidence: 99%

Macromolecular association of ADP-ribosyltransferase and its correlation with enzymic activity

Bauer

Büki

Hakam

et al. 1990

Biochemical Journal

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The macromolecular self-association of ADP-ribosyltransferase protein in solution was studied by several experimental techniques: quantitative gel filtration, electrophoretic analyses in non-denaturing gels, and cross-linking the enzyme protein with glutaraldehyde, dimethyl pimelimidate, dimethyl suberimidate, dimethyl 3,3'-dithiobisproprionimidate and tetranitromethane. The self-association of the polypeptide components obtained by plasmin digestion was also determined by using the above cross-linking agents. Monomers and cross-linked dimers of the enzyme protein, possessing enzymic activity, were separated in non-denaturing gels by electrophoresis. The basic polypeptide fragments, exhibiting molecular masses of 29 kDa and 36 kDa, self-associated, whereas the polypeptides with molecular masses of 56 kDa and 42 kDa associated only to a negligible extent, indicating that the peptide regions that also bind DNA and histones are probable sites of self-association in the intact enzyme molecule. Macromolecular association of the enzyme was indicated by a protein-concentration-dependent red-shift in protein fluorescence. The specific enzymic activity of the isolated ADP-ribosyltransferase depended on the concentration of the enzyme protein, and at 2.00 microM concentration the enzyme was self-inhibitory. Dilution of the enzyme protein to 30-40 nM resulted in a large increase in its specific activity. Further dilution to 1-3 nM coincided with a marked decrease of specific activity. Direct enzymic assays of electrophoretically separated monomers and cross-linked dimers demonstrated that the dimer appears to be the active molecular species that catalyses poly(ADP-ribose) synthesis. The NAD+ glycohydrolase activity of the enzyme was also dependent on protein concentration and was highest at 1-3 nM enzyme concentration, when polymerase activity was minimal, indicating that the monomeric enzyme behaved as a glycohydrolase, whereas poly(ADP-ribosyl)ation of enzyme molecules was maximal when the enzyme tends to be self-associated to the dimeric form.

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Section: Discussionmentioning

confidence: 99%

Macromolecular association of ADP-ribosyltransferase and its correlation with enzymic activity

Bauer

Büki

Hakam

et al. 1990

Biochemical Journal

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Poly(ADP‐ribosylation) of atypical CS histone variants is required for the progression of S phase in early embryos of sea urchins

Imschenetzky

Montecino

Puchi

1991

J of Cellular Biochemistry

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The patterns of poly(ADP-ribosylation) in vivo of CS (cleavage stage) histone variants were compared in sea urchin zygotes at the entrance and the exit of S1 and S2 in the initial developmental cell cycles. This post-translational modification was detected by Western immunoblots with rabbit sera anti-poly(ADP-ribose) that was principally reactive against ADP-ribose polymers and slightly against ADP-ribose oligomers. The effect of 3 aminobenzamide (3-ABA), an inhibitor of the poly(ADP-ribose) synthetase, on S phase progression was determined in vivo by measuring the incorporation of 3H thymidine into DNA. The results obtained indicate that the CS histone variants are poly(ADP-ribosylated) in a cell cycle dependent manner. A significantly positive reaction of several CS variants with sera anti-poly(ADP-ribose) was found at the entrance into S phase, which decreases after its completion. The incubation of zygotes in 3-ABA inhibited the poly(ADP-ribosylation) of CS variants and prevented both the progression of the first S phase and the first cleavage division. These observations suggest that the poly(ADP-ribosylation) of atypical CS histone variants is relevant for initiation of sea urchin development and is required for embryonic DNA replication.

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Applications of Permeabilization

Bánfalvi

2016

Permeability of Biological Membranes

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Cellular regulation of ADP-ribosylation of proteins

Cited by 10 publications

References 36 publications

Macromolecular association of ADP-ribosyltransferase and its correlation with enzymic activity

Macromolecular association of ADP-ribosyltransferase and its correlation with enzymic activity

Poly(ADP‐ribosylation) of atypical CS histone variants is required for the progression of S phase in early embryos of sea urchins

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