Search

PERSPECTIVES AND SUMMARY S82 ROLE OF GANGLIOSIDE GMI AS THE CELL SURFACE RECEPTOR FOR CHOLERAGEN ......... ...... . . . ....... . ......... ...... .... 583 Interaction of Gangliosides and Their Oligosaccharides with Choleragen and Its Subunits 584 Activation of Adenylate Cyclase by Choleragen in Intact Cells 585 Activation of Adenylate Cyclase by Choleragen in Cell-Free Systems . 587 REQUIREMENTS FOR DEMONSTRATION OF ADENYLATE CYCLASE ACTIVATION BY CHOLERAGEN IN CELL-FREE SySTEMS ....... . .. 588 NAD !i88 GTP 588 Calcium-Dependent Regulatory Protein 589 ROLE OF NAD AS SUBSTRATE IN REACTIONS CATALYZED BY CHOLERAGEN 589 Mechanism of Action of NAD-Dependent Pseudomonas EXotoxin A and Diphtheria Toxin .... . . . ....... ..... ......... 590 NAD Glycohydrolase and ADP-Ribosyltransferase Activities oj Choleragen 591 Effects ofCholeragen on GTP-Binding Protein and GTPase Activity 592 SIMILARITIES BETWEEN CHOLERAGEN AND ESCHERICHIA COLI HEAT-LABILE ENTEROTOXIN 593 AN ADP-RIBOSYLTRANSFERASE FROM TURKEY ERYTHROCYTES WITH CHOLERAGEN-LIKE ACTIVITy .... . . . . . . . . . . . 595

Publisher Summary This chapter analyzes poly(ADP-ribose) and ADP-ribosylation of proteins. Poly(ADP-ribose) and the ADP-ribosylation of proteins constitute a novel type of covalent modification of proteins. They are ubiquitously distributed in nature and are implicated in the regulation of cell proliferation, protein synthesis, and DNA as well as RNA metabolism. This type of post-translational modification is unique because NAD, nicotinamide adenine dinucleotide, whose primary function is an electron carrier in biological oxidation, invariably provides the ADP-ribosyl moiety, which is transferred on to a protein molecule. The ADP-ribosyl unit thus, covalently attached to a protein acceptor is present as either a monomer or a polymer as in the case of the nuclear system. This chapter also summarizes developments in this field of research and some experimental results. It reviews briefly, mono ADP-ribosylation of proteins, in which only a single ADP-ribosyl moiety is transferred to a protein acceptor. It also covers a more complex reaction, poly(ADP-ribose) in nuclei, in which the ADP-ribosyl units are polymerized.