By Miguel Molinete, Valérie Schreiber, Frédéric Simonin, Gérard Gradwohl (auth.), Guy G. Poirier, Pierre Moreau (eds.)
This monograph is devoted to at least one of the discoverers of poly(ADP ribose), Professor Paul Mandel, from the Centre de Neurochimie in Strasbourg. we want to congratulate him for his exceptional contributions to the sphere of poly(ADP-ribosyl)ation and convey our gratitude for his aid within the final years and especially for his encouragement for the association of this assembly. Poly(ADP-ribose) was once came across greater than 25 years in the past. in view that then, very good development has been made at the examine of the mechanisms of poly(ADP ribose) response. The final 5 years were relatively fascinating because the improvement of assorted molecular biology innovations has printed the complicated nature of this multifunctional enzyme. taking a look at the contributions offered at this assembly, it turns into seen that extra paintings on the molecular point is required. probably, those experiments will shed a few gentle at the services of poly(ADP-ribose), yet additional ~iophysical experiences will nonetheless be required to completely comprehend this advanced enzymatic system.
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Gene 90, 249-254. Ittel, M. P. (1991). Chicken poly(ADP-ribose) polymerase: complete sequence deduced from cDNA, comparison with mammalian enzyme sequences. G. and Moreau, P. (1989). Cloning of rodent cDNA encoding the poly(ADP-ribose) polymerase catalytic domain and analysis of mRNA levels during the cell cycle. Biochem. Cell Bioi. 67, 653-660. L. A. (1988). Nucleotide sequence of the gene of vesicular somatis virus (New Jersey): identification of conserved domains in the New Jersey and Indiana L proteins.
This experiment was extremely interesting also from another point of view: S. cerevisiae does not show ADP-ribosyJation in detectable amounts, thereby raising the question if this organism would react to the action of human pADPRT expressed in this system. Expression pJasmids, containing the pADPRT cDNA and portions thereof in various orientations,were constructed as depicted in Fig. 1. Not I Noli YpADPRT. ;... - ... "...................................... :5~! ~!! ~ ~ ~ ~ A YpADPRTGa' Net I Fig.
Althaus, F. , Richter, C. (1987). ADP-ribosylation of proteins. : ADP-ribosyltransferase from Helix pomatia. Purification and characterization. I. 248, 859-864 (1987). : ADP-ribosyltransferase is highly conserved: purification and characterization of ADP-ribosyltransferase from a fish and its comparison with the human enzyme. B. 157, 567-572 (1987). : (Induction of murine teratocarcinoma cell differentiation by suppression of poly (ADP-ribose) synthesis. ScLUSA 81,7132-7136 (1984). 424-428, Springer Verlag, Berlin (1985).