By Friedrich Haag, Friedrich Koch-Nolte
Introduction. Mono(ADP-ribosyl)Transferases and comparable Enzymes: rising Gene households; F. Koch-Nolte, F. Haag.Mono-ADP-ribosylationin Prokaryotes. Crystal constitution of Diphtheria Toxin guaranteed to Nicotinamide Adenine Dinucleotide; C.E. Bell, D. Eisenberg.MolecularApproaches to Eukaryotic Mono(ADP-ribosyl)Transferases. series and Structural hyperlinks among far-off ADp-ribosyltransferase households; F.Bazan, F. Koch-Nolte.Moni(ADP-ribosyl)Transferases within the ImmuneSystem. legislation of Cytotoxic T mobilephone capabilities by way of a GPI-anchored Ecto-ADP-ribosyltransferase; J. Wang, et al.Mono-ADP-ribosylation inOther Animal Tissues. An ADP-Ribosyltransferase from Bovine Erythrocytes it seems that particular for Cysteine Residues; S. vanHeyningen, B. Saxty.Physiology of GPI-Anchored Proteins. mobilephone floor Dynamics of GPI-anchored Proteins; F.R. Maxfield, S. Mayor.Relationship of ADP-Ribosyltransferases to NAD+ Glycohydrolasesand ADP-ribosyl Cyclases. ADp-Ribose in Glycation and Glycoxidation Reactions; E.L. Jacobson, et al.Special Lecture Commemorating theRetirement of Professor Heinz-Gunter Thiele. Appendix. 28 extra Lectures. 24 Poster studies. Index.
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Extra resources for ADP-Ribosylation in Animal Tissues: Structure, Function, and Biology of Mono (ADP-ribosyl) Transferases and Related Enzymes
Cholera toxin for instance, exhibits catalytic properties which according to Moss and Vaughan (18), not only comprise ADP-ribosyl transferase activity. The toxin also acts as a NAD+ glycohydrolase, and it is able to perform an automodification. Furthermore, choleragen responds to the help of GTP-binding proteins, the ARF' s, with increased activity (8), The first toxin found to produce its effect as an ADP-ribosyltransferase was actually diphtheria toxin. Apparently primed by the detection of the poly-ADP-ribosylating system in cell nuclei, the Hayaishi group made a good guess in assuming that the NAD+ requirement for the toxin's action was due to an ADP-ribosyltransferase reaction modifying elongation factor 2 (19).
Receptor 5: 43-49. 27. C, R. Walseth. 1995. Cyclic ADP-ribose and its metabolic enzymes. Biochimie 77:345-355. 28. Zhang F, Q. Gu, P. Sih. 1995. Enzymatic cyclization of nicotinamide adenine dinucleotide phosphate (NADP). Chem. Lellers 5: 2267-2272; 29. , P. Lu. KJacobson. 1995. 2'-Phospho cyclic ADP-ribose, a calcium-mobilizing agent derived from NADP. 1. Bioi. Chem. 27/:4747--4754. 30. C, S. Kabra, A. Bazan, G. CHoward. 1995. CD38-Mediated Ribosylation of Proteins. 1. Immunol. 155: 812-817. 3 ADP-RIBOSYLARGININE HYDROLASES AND ADP-RIBOSYLTRANSFERASES Partners in ADP-Ribosylation Cycles Joel Moss, Anna Zolkiewska, and Ian Okazaki Pulmonary-Critical Care Medicine Branch National Heart, Lung, and Blood Institute National Institutes of Health Bethesda, Maryland 20892 ABSTRACT Mono-ADP-ribosylation is a reversible modification of arginine residues in proteins, with NAD:arginine ADP-ribosyltransferases and ADP-ribosylarginine hydrolases constituting opposing arms of a putative ADP-ribosylation cycle.
Indeed, impressive results have been obtained by the group at the Abteilung fUr Immunologie (cf. 22 and Table II. Only two of their highlights are listed here). Additional fascinating stories are emerging in the field of mono-ADP-ribosylation processes, like protein traffic through membranes, which includes the physiological function of ARF (cf. 23) and possibly the reversible ADP-ribosylation ofa new class ofG-proteins as discovered with the aid of Brefeldin A (23). Consider also the recent detection of an entire new class of ADP-ribosyl proteins by Jacobson et al.