title: Vertebrate mono-ADP-ribosyltransferases.
abstract: Mono-ADP-ribosylation appears to be a reversible modification of proteins, which occurs in many eukaryotic and prokaryotic organisms. Multiple forms of arginine-specific ADP-ribosyltransferases have been purified and characterized from avian erythrocytes, chicken polymorphonuclear leukocytes and mammalian skeletal muscle. The avian transferases have similar molecular weights of approximately 28 kDa, but differ in physical, regulatory and kinetic properties and subcellular localization. Recently, a 38-kDa rabbit skeletal muscle ADP-ribosyltransferase was purified and cloned. The deduced amino acid sequence contained hydrophobic amino and carboxy termini, consistent with known signal sequences of glycosylphosphatidylinositol (GPI)-anchored proteins. This arginine-specific transferase was present on the surface of mouse myotubes and of NMU cells transfected with the cDNA and was released with phosphatidylinositol-specific phospholipase C. Arginine-specific ADP-ribosyltransferases thus appear to exhibit considerable diversity in their structure, cellular localization, regulation and physiological role.
authors.affiliation: Laboratory of Cellular Metabolism, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892.
authors.forename: A
authors.initials: A
authors.lastname: Zolkiewska
authors.forename: I J
authors.initials: IJ
authors.lastname: Okazaki
authors.forename: J
authors.initials: J
authors.lastname: Moss
mesh_terms: D036002:ADP Ribose Transferases; D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine; D001717:Birds / Q000378:metabolism*; D002467:Cell Nucleus / Q000201:enzymology; D008099:Liver / Q000201:enzymology / Q000648:ultrastructure; D008322:Mammals / Q000378:metabolism*; D008969:Molecular Sequence Data; D009132:Muscles / Q000201:enzymology; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*
chemical_list: D001120:Arginine; D036002:ADP Ribose Transferases; D011065:Poly(ADP-ribose) Polymerases