Target protein for eucaryotic arginine-specific ADP-ribosyltransferase.
Among ADP-ribosyltransferases reported in eucaryotes, arginine-specific transferases from turkey erythrocytes, chicken heterophils and rabbit skeletal muscle have been purified and extensively studied. They were reported to modify a number of proteins in vitro. ADP-ribosylation of Ha-ras-p21 and transducin by the turkey erythrocyte transferase inhibits their GTPase and GTP-binding activities. Chicken heterophil enzyme modifies several substrate proteins for protein kinases and decreases the phosphate-acceptor activity. Rabbit skeletal muscle Ca(2+)-ATPase is inhibited by ADP-ribosylation catalyzed by the muscle transferase. Three transferases all ADP-ribosylate small molecular weight guanidino compounds such as arginine, arginine methylester and agmatine and poly-L-arginine and nuclear histones. However, the observation that muscle transferase did not ADP-ribosylate casein or actin, both of which can be modified by the heterophil transferase under the same conditions indicates that substrate specificity of these two enzymes are different. Substrate-dependent effects were observed with polyions of nucleotides such that polyanions stimulate the ADP-ribosylation of possible target protein, p33 by chicken heterophil transferase but has no effect on the modification of casein by the same enzyme.
Tsuchiya
M
M
Department of Biochemistry, Shimane Medical University, Izumo, Japan.
Shimoyama
M
M
D000818:Animals; D001120:Arginine; D002645:Chickens / Q000378:metabolism*; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D011817:Rabbits / Q000378:metabolism*; D013379:Substrate Specificity; D014422:Turkeys / Q000378:metabolism*
D011506:Proteins; D001120:Arginine; D011065:Poly(ADP-ribose) Polymerases