By Dr. Felix R. Althaus, Dr. Christoph Richter (auth.)
In 1966, a paper entitled "On the formation of a unique adenylylic compound by means of enzymatic extracts of liver nuclei" from Paul Mandel's laboratory in Strasbourg, France, planted the seed for a swiftly starting to be new box of organic study targeting ADP-ribosylation reactions. the advance of this box over the last 2 a long time displays a great deal a contemporary development of organic learn. As extra exact wisdom accumulates, enigmatic phenomena develop into recommendations which create their very own enigmata. This strategy has a tendency to prefer the advance of a number of, possible disconnected, examine traces until eventually simplicity emerges from chaos and unifying thoughts alternative for controversy. it seems that the sphere of ADP-ribosylation reactions has now not but attained this latter level. for instance, with the id of 2 various periods of ADP-ribosylation reactions, i.e., mono-ADP-ribosyla tion and poly-ADP-ribosylation reactions, the sector cut up very early into separate branches of analysis. With the current quantity, we now have divided the duty of reviewing those periods of ADP ribosylation for this reason, even supposing their coexistence in eukaryotes may well contain a more in-depth useful linkage than hitherto recognized.
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Extra info for ADP-Ribosylation of Proteins: Enzymology and Biological Significance
Neurochem Res 6:1253-1263 Bizec JC, Klethi J, Mandel P (1985) Poly(ADP-ribosyl) polymerase du cristallin de bovide; modulation de son activite au cours du vieillissement. CR Acad Sci 300:37-41 Brightwell MO, Leech CE, O'Farrell MK, Wish WJD, Shall S (1975) Poly(adenosine diphosphate ribose) polymerase in physarum polycephalum. Biochem J 1476:119-129 Brkic G, Topaloglou A, Altmann H (1985) Poly(ADP-ribose) in nucleoids. In: Althaus FR, Hilz H, Shall S (eds) ADP-ribosylation of proteins. Springer, Berlin Heidelberg New York Tokyo, pp 217-221 Burtscher H, Auer B, Klocker H, Schweiger H, Hirsch-Kauffmann H (1986) Isolation of ADPribosyltransferase by affinity chromatography.
Enzymic formation from nicotinamide adenine dinucleotide in mammalian nuclei. J Bioi Chern 242:3164-3171 Nishizuka Y, Veda K, Yoshihara K, Yamamura H, Takeda M, Hayaishi 0 (1969) Enzymic adenosine diphosphoribosylation of nuclear proteins. Cold Spring Harbor Symp Quant Bioi 34:781-786 Nolan NL, Kidwell WR (1982) Effect of heat shock on poly(ADP-ribose) synthetase and DNA repair in Drosophila cells. Radiat Res 90:187-203 Ohashi Y, Veda K, Hayaishi 0, Ikai K, Niwa D (1984) Induction of murine teratocarcinoma cell differentiation by suppression ofpoly(ADP-ribose) synthesis.
1). Similar results were recently reported by Tanuma et al. (1986b). Using HeLa cells, they identified a tightly bound nuclear glycohydrolase activity and a soluble cytosolic activity, which differed in their Mr, Km, and pH and salt requirements for maximal activity. , enucleated) human red blood cells (Tanuma et al. 1). Since the ADP-ribosyl residues of poly(ADP-ribose) are linked through an (1"-+2') alpha anomeric glycosidic bond (cf. Chap. 1), the enzyme may also be termed a(1"-+2')poly(ADP-ribose) ribohydrolase.