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Mono ADP-ribosylation

Researchers found that NAD serves as a substrate in poly(ADP-ribose) synthesis, a reaction important for DNA repair processes. In addition, it takes part in mono (ADP-ribosyl)ation reactions that are involved in endogenous regulation of many aspects of signal transduction and membrane trafficking in eukaryotic cells. [Pg.851]

Banasik M, Komura H, Shimoyama M, Ueda K (1992) Specific inhibitors of poly(ADP-ribose) synthetase and mono(ADP-ribosyl)transferase. J Biol Chem 267 1569-1575... [Pg.64]

Figure 2 The actin-ADP-ribosylating toxins, (a) Molecular mode of action. The actin-ADP-ribosylating toxins covalently transfer an ADP-ribose moiety from NAD+ onto Arg177 of G-actin in the cytosol of targeted cells. Mono-ADP-ribosylated G-actin acts as a capping protein and inhibits the assembly of nonmodified actin into filaments. Thus, actin polymerization is blocked at the fast-growing ends of actin filaments (plus or barbed ends) but not at the slow growing ends (minus or pointed ends). This effect ultimately increases the critical concentration necessary for actin polymerization and tends to depolymerize F-actin. Finally, all actin within an intoxicated cell becomes trapped as ADP-ribosylated G-actin. Figure 2 The actin-ADP-ribosylating toxins, (a) Molecular mode of action. The actin-ADP-ribosylating toxins covalently transfer an ADP-ribose moiety from NAD+ onto Arg177 of G-actin in the cytosol of targeted cells. Mono-ADP-ribosylated G-actin acts as a capping protein and inhibits the assembly of nonmodified actin into filaments. Thus, actin polymerization is blocked at the fast-growing ends of actin filaments (plus or barbed ends) but not at the slow growing ends (minus or pointed ends). This effect ultimately increases the critical concentration necessary for actin polymerization and tends to depolymerize F-actin. Finally, all actin within an intoxicated cell becomes trapped as ADP-ribosylated G-actin.
The binary nature of iota toxin from C. perfringens type E was first explored in 1986 by Stiles and Wilkins. The overall mode of action for iota toxin is widely comparable to C2 toxin. The binding/translocation component iota b (Ib) facilitates cellular uptake of the enzyme component iota a (la) in a like manner as previously described for C2 toxin. la, just as C2I, specifically mono-ADP-ribosylates G-actin at Argl77. ... [Pg.156]

Kots, A. Y., Skurat, A. V., Serienko, E. A., Bulargina, T. V., and Severin, E. S. (1992). Nitric oxide stimulates the cysteine-specific mono(ADP-ribosylation) of glyceralde-hyde-3-phosphate dehydrogenase from human. erythrocytes. FEBS Lett. 300, 9-12. Kowaluk, E. A., and Fung, H. L. (1990). Spontaneous liberation of nitric oxide cannot account for in vitro vascular relaxation by S-nitrosothiols. J. Pharmacol. Exp. Ther. 255,... [Pg.76]

Yuan, J., Huiatt, T. W., Liao, C. X., Robson, R. M., and Graves, D.J. (1999). The effects of mono-ADP-ribosylation on desmin assembly-disassembly Determination of the chemical features of bound ADP-ribose that prevent desmin filament formation. [Pg.142]

NAD is the source of ADP-ribose for the modification of proteins by mono-ADP-ribosylation, catalyzed by ADP-ribosyltransferases (Section 8.4.2), and poly(ADP-ribosylation), catalyzed by poly(ADP-ribose) polymerase (Section 8.4.3). It is also the precursor of two second messengers that act to increase the intracellular concentration of calcium, cADP-ribose, and nicotinic acid adenine dinucleotide phosphate (Section 8.4.4). [Pg.214]

Zolkiewska A, Okosaki IJ, Moss J (1994) Vertebrate mono-ADP-ribosyl-transferases. In Mo/. Cell. Biochem. 138 107-112. [Pg.17]

Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. In Nature (London) 340 680-685 Laugwitz KL, Spicher K, Schultz G et al. (1994) Identification of receptor-activated G proteins selective immunoprecipitation of photolabeled G-protein a subunits. In Methods Enzymol. 237 283-294 Meyer T, Hilz H (1986) Production of anti-(ADP-ribose) antibodies with the aid of a dinucleotide-pyrophosphatase-resistent hapten and their application for the detection of mono(ADP-ribosyl)ated polypeptides. In Ear. J. Biochem. 155 157-165... [Pg.61]

Simpson LL, Stiles BG, Zepeda H etal. (1989) Production by Clostridium spiroforme of an iotalike toxin that possesses mono(ADP-ribosyl)transferase activity Identification of a novel class of ADP- ribosyltransferases. In Infect. Immun. 57 255-61 Stiles BG, Wilkens TD (1986) Purification and characterization of Clostridium perfringens iota toxin dependence on two nonlinked proteins for biological activity. In Infect. Immun. 54 683-8... [Pg.100]

Mono(ADP-ribosyl)ation Reactions Bacterial ADP-ribosylating Toxins Concluding Remarks and Future Prospects... [Pg.305]

When a single ADP-ribose moiety (n = 1) becomes attached to an acceptor site, the reaction is referred to as mono(ADP-ribosyl)ation, and when a homopolymer chain of repeating units is attached, the process is referred to as poly(ADP-ribo-syl)ation (n > 1). Polymer chains may consist of over 200 ADP-ribose residues and may also contain branches, occurring some three times per 100 residues (see Figure 1). [Pg.307]

These bonds are characteristic of the various mono(ADP-ribosyl) transferase catalyzed reactions that are known (see section on mono(ADP-ribosyl)ation reactions below). [Pg.308]

Mitochondrial ADP-ribosylation. Other protein substrates for mono(ADP-ribosyl) transferases continue to be reported, but the best characterized reaction is that of mammalian cell mitochondria. Most mono-ADP-ribosyl-protein conjugates in eukaryotic cells are associated with mitochondria. A specific function, namely, stimulation of calcium release from mitochondria, has been ascribed to ADP-ribosylation activity in this organelle. This could, therefore, be an important cell regulatory mechanism, since numerous calcium-dependent enzymes play an important role in cell functioning. [Pg.319]

The use of bacterial toxins as molecular probes will continue to provide valuable information on the functions of their various substrates. In addition, studies on endogenous cellular mono(ADP-ribosyl) transferases look set to expand. New substrates will be identified and the biochemical consequences of the different modifications will reveal the roles played by mono(ADP-ribosylation) reactions in different cell compartments. For example, the case of cytoskeletal actin has been discussed (see Figure 8). Work in Mandel s laboratory (Mandel, 1992) has revealed that other cytoskeletal proteins are also substrates for endogenous ADP-ribosyl transferase, including components of the microfilaments (tubulin, intermediate filaments, and the neurofilament proteins L, M, and H). [Pg.320]

Richter, C., Frei, B., Schlegel, J. (1985). Calcium transport and mono(ADP-ribosylation) in mitochondria. In ADP-Ribosylation of Proteins (Althaus, F. R., Hilz, H., Shall, S., Eds.), pp. 530-535. Springer-Verlag, Berlin. [Pg.321]

Tsuyama, S., Fujita, H., Hijikata, R., Okamoto, H., and Takanaks, S., Effects of mono-ADP-ribosylation on cytoskeletal actin in chromaffin cells and their release of catecholamine, Int. J. Biochem. Cell Biol., 31, 601, 1999. [Pg.328]

Yamashita and co-workers reported that nicotinamide exhibit attaching repellent activity against the blue mussel (Mytilus edulis) [119]. Nicotinamide (34) is a product of NAD+ cleavage by mono (ADP-ribosyl) transferase, and it serves as an effective inhibitor of the enzyme activity... [Pg.1097]

The NAD -dependent modification of GAPDH originally was thought to be identical to mono-ADP-ribosylation. Although NO-induced GAPDH modification resembles some features of ADP-ribosylation reactions, conditions for optimal protein modification are different from those in the toxin-... [Pg.355]

Mono- and poly-ADP-ribosylation. Mono-ADP-ribosylation and poly(ADP-ribose) modification catalyzed by ADP-ribosyl transferase and poly(ribose) synthetase respectively, append mono- and poly ADP-ribose (ADPR) moieties (Hayaishi and Ueda, 1977). In poly ADPR, the polymeric chain consists of woADP-ribose, 2 -(5"-phosphoribosyl)-5 -AMP... [Pg.486]

Mendoza-Alvarez H, Alvarez-Gonzalez R. Biochemical characterization of mono(ADP-ribosyl)ated poly(ADP-ribose) polymerase. Biochemistry (USA) 1999 38 3948-3953. [Pg.66]

The transfer of the ADP-ribose moiety from NAD onto a biological macromolecule (in almost all cases an amino acid side chain of a protein) is referred to as ADP-ribosylation. Subsequently, another ADP-ribose unit can be attached to the protein-bound ADP-ribose. Further elongation of the ADP-ribose chain will result in poly-ADP-ribosylation. This process will not be further addressed in this chapter. However, mono-ADP-ribosylation, i.e., attachment of a single ADP-ribose unit to a protein, has also been established as a specific protein modification with important r ulatory functions. [Pg.133]

In mammalians, mono-ADP-ribosylation appears to take place primarily on the surface of immune cells. The corresponding transferases are either anchored in the plasma membrane via glycosylphosphatidylinositol (GPI) or secreted. For example, in the lung, the antimicrobial function of a-defensin-1, which is secreted by immune cells, is diminished by mono-ADP-ribosylation. ... [Pg.133]

Corda D, Di Girolamo M. Functional aspects of protein mono-ADP-ribosylation. EMBO J 2003 22 1953-1958. [Pg.138]

See other pages where Mono ADP-ribosylation is mentioned: [Pg.153]    [Pg.155]    [Pg.155]    [Pg.226]    [Pg.136]    [Pg.94]    [Pg.118]    [Pg.678]    [Pg.307]    [Pg.318]    [Pg.320]    [Pg.52]    [Pg.330]    [Pg.83]    [Pg.133]    [Pg.133]    [Pg.134]   
See also in sourсe #XX -- [ Pg.486 ]



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