Mono-ADP-ribosylation: A Reversible Posttranslational Modification of Proteins

Advances in Pharmacology

Volumn 35, Issue C, 1996, Pages 247-280

  Okazaki, Ian J ^a   Moss, Joel ^a  

^a NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE;

AMINO ACID SEQUENCE; DRUG ANTAGONISM; MOLECULAR GENETICS; REVIEW;

ADP RIBOSE TRANSFERASES; AMINO ACID SEQUENCE; MOLECULAR SEQUENCE DATA;

EID: 0029681933     PISSN: 10543589     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1054-3589(08)60277-X     Document Type: Article

References (149)

1. Aktories K. Clostridial ADP-ribosylating toxins: Effects on ATP and GTP-binding proteins. Mol. Cell. Biochem. 138 (1994) 167-176
2. Aktories K., Barmann M., Ohishi I., Tsuyama S., Jakobs K.G., and Habermann E. Botulinum C2 toxin ADP-ribosylates actin. Nature (London) 322 (1986) 390-392
3. Allured V.S., Collier R.J., Carroll S.F., and McKay D.B. Structure of exotoxin A of Pseudomonas aeruginosa at 3.0-Angstrom resolution. Proc. Natl. Acad. Sci. U.S.A. 83 (1986) 1320-1324
4. Alvarez-Gonzalez R., Pacheco-Rodriguez G., and Mendoza-Alvarez H. Enzymology of ADP-ribose polymer synthesis. Mol. Cell. Biochem. 138 (1994) 33-37
5. Antoine R., and Locht C. The NAD-glycohydrolase activity of the pertussis toxin S1 subunit: Involvement of the catalytic His-35 residue. J. Biol. Chem. 269 (1994) 6450-6457
6. Antoine R., Tallett A., vanHeyningen S., and Locht C. Evidence for a catalytic role of glutamic acid 129 in the NAD-glycohydrolase activity of the pertussis toxin S1 subunit. J. Biol. Chem. 268 (1993) 24149-24155
7. Banasik M., Komura H., Shimoyama M., and Ueda K. Specific inhibitors of poly(ADP-ribose) synthetase and mono(ADP-ribosyl)transferase. J. Biol. Chem. 267 (1992) 1569-1575
8. Banasik M., and Ueda K. Inhibitors and activators of ADP-ribosylation reactions. Mol. Cell. Biochem. 138 (1994) 185-197
9. Barbieri J.T., Mende-Mueller L.M., Rappuoli R., and Collier R.J. Photolabeling of Glu-129 of the S1 subunit of pertussis toxin with NAD. Infect. Immun. 57 (1989) 3549-3554
10. Blanke S.R., Huang K., Wilson B.A., Papini E., Covacci A., and Collier R.J. Active-site mutations of diphtheria toxin catalytic domain: Role of histidine-21 in nicotinamide adenine dinucleotide binding and ADP-ribosylation of elongation factor 2. Biochemistry 33 (1994) 5155-5161
11. Blanke S.R., Huang K., and Collier R.J. Active-site mutations of diphtheria toxin: Role of tyrosine-65 in NAD binding and ADP-ribosylation. Biochemistry 33 (1994) 15494-15500
12. Braun U., Habermann B., Just I., Aktories K., and Vandekerckhove J. Purification of the 22-kDa protein substrate of botulinum ADP-ribosyltransferase C3 from porcine brain cytosol and its characterization as a GTP-binding protein highly homologous to the rho gene product. FEBS Lett. 243 (1989) 70-76
13. Burnette W.N., Cieplak W., Mar V.L., Kaljot K.T., Sato H., and Keith J.M. Pertussis toxin S1 mutant with reduced enzyme activity and a conserved protective epitope. Science 242 (1988) 72-74
14. Burnette W.N., Mar V.L., Platler B.W., Schlotterbeck J.D., McGinley M.D., Stoney K.S., Rohde M.F., and Kaslow H.R. Site-specific mutagenesis of the catalytic subunit of cholera toxin: Substitution lysine for arginine 7 causes loss of activity. Infect. Immun. 59 (1991) 4266-4270
15. Burstein D., Mordes J.P., Greiner D.L., Stein D., Nakamura N., Handler E.S., and Rossini A.A. Prevention of diabetes in BB/Wor rat by single transfusion of spleen cells. Parameters that affect degree of protection. Diabetes 38 (1989) 24-30
16. Carroll S.F., and Collier R.J. Active site of Pseudomonas aeruginosa exotoxin A. Glutamic acid 553 is photolabeled by NAD and shows functional homology with glutamic acid 148 of diphtheria toxin. J. Biol. Chem. 262 (1987) 8707-8711
17. Carroll S.F., and Collier R.J. Amino acid sequence homology between the enzymic domains of diphtheria toxin and pseudomonas aeruginosa exotoxin A. Mol. Microbiol. 2 (1988) 293-296
18. Carroll S.F., McCloskey J.A., Crain P.F., Oppenheimer N.J., Marschner T.M., and Collier R.J. Photoaffinity labeling of diphtheria toxin fragment A with NAD: Structure of the photoproduct at position 148. Proc. Natl. Acad. Sci. U.S.A. 82 (1985) 7237-7241
19. Chang Y.-C., Soman G., and Graves D.J. Identification of an enzymatic activity that hydrolyzes protein-bound ADP-ribose in skeletal muscle. Biochem. Biophys. Res. Commun. 139 (1986) 932-939
20. Choe S., Bennett M.J., Fujii G., Curmi P.M.G., Kantardjieff K.A., Collier R.J., and Eisenberg D. The crystal structure of diphtheria toxin. Nature (London) 357 (1992) 216-222
21. Collier R.J. Diphtheria toxin: Structure and function of a cytocidal protein. In: Moss J., and Vaughan M. (Eds). "ADP-ribosylating Toxins and G Proteins: Insights into Signal Transduction" (1990) 3-19
22. De Matteis M.A., DiGirolamo M., Colanzi A., Pallas M., DeTullio G., McDonald L.J., Moss J., Santini G., Bannykh S., Corda D., and Luini A. Stimulation of endogenous ADP-ribosylation by brefeldin A. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 1114-1118
23. Domenighini M., Montecucco C., Ripka W.C., and Rappuoli R. Computer modelling of the NAD binding site of ADP-ribosylating toxins: active-site structure and mechanism of NAD binding. Mol. Microbiol. 5 (1991) 23-31
24. Domenighini M., Magagnoli C., Pizza M., and Rappuoli R. Common features of the NAD-binding and catalytic site of ADP-ribosylating toxins. Mol. Microbiol. 14 (1994) 41-50
25. sα activity and abundance. Biochem. J. 288 (1992) 331-336
26. Douglas C.M., and Collier R.J. Exotoxin A of Pseudomonas aeruginosa: Substitution of glutamic acid-553 with aspartic acid drastically reduces toxicity and enzymic activity. Infect. Immun. 169 (1987) 4967-4971
27. Doukas J., and Mordes J.P. T lymphocytes capable of activating endothelial cells in vitro are present in rats with autoimmune diabetes. J. Immunol. 150 (1993) 1036-1046
28. Duman R.S., Winston S.M., Clark J.A., and Nestler E.J. Corticosterone regulates the expression of ADP-ribosylation factor messenger RNA and protein in rat cerebral cortex. J. Neurochem. 55 (1990) 1813-1816
29. Duman R.S., Terwilliger R.Z., and Nestler E.J. Endogenous ADP-ribosylation in brain: Initial characterization of substrate proteins. J. Neurochem. 57 (1991) 2124-2132
30. +-mediated stimulation of adenylate cyclase in cardiac membranes. Biochem. Biophys. Res. Commun. 142 (1987) 631-637
31. Gerber L.D., Kodukula K., and Udenfriend S. Phosphatidylinositol glycan (PI-G) anchored membrane proteins. Amino acid requirements adjacent to the site of cleavage and PI-G attachment in the COOH-terminal signal peptide. J. Biol. Chem. 267 (1992) 12168-12173
32. Godeau F., Belin D., and Koide S.S. Mono(adenosine diphosphate ribosyl) transferase in Xenopus tissues. Direct demonstration by a zymographic localization in sodium dodecyl sulfate-polyacrylamide gels. Anal. Biochem. 137 (1984) 287-296
33. Greiner D.L., Handler E.S., Nakano K., Mordes J.P., and Rossini A.A. Absence of the RT-6 T cell subset in diabetes-prone BB/W rats. J. Immunol. 136 (1986) 148-151
34. Hawkins D.J., and Browning E.T. Tubulin adenosine diphosphate ribosylation is catalyzed by cholera toxin. Biochemistry 21 (1982) 4474-4479
35. Jacobson M.K., Loflin P.T., Aboul-Ela N., Mingmuang M., Moss J., and Jacobson E.L. Modification of plasma membrane protein cysteine residues by ADP-ribose in vivo. J. Biol. Chem. 265 (1990) 10825-10828
36. Johnson V.G., and Nicholls P. Histidine-21 does not play a major role in diphtheria toxin catalysis. J. Biol. Chem. 269 (1994) 4349-4354
37. Jung M., Just I., vanDamme J., Vandekerckhove J., and Aktories K. NAD-binding site of the C3-like ADP-ribosyltransferase from Clostridium limosum. J. Biol. Chem. 268 (1993) 23215-23218
38. Just I., Sehr P., Jung M., vanDamme J., Puype M., Vandekerckhove J., Moss J., and Aktories K. ADP-ribosyltransferase type A from turkey erythrocytes modifies actin at arg-95 and arg-372. Biochemistry 34 (1995) 326-333
39. Just I., Selzer J., Jung M., vanDamme J., Vandekerckhove J., and Aktories K. Rho-ADP-ribosylating exoenzyme from Bacillus cereus. Purification, characterization, and identification of the NAD-binding site. Biochemistry 34 (1995) 334-340
40. Kaslow H.R., Schlotterbeck J.D., Mar V.L., and Burnette N.W. Alkylation of cysteine 41, but not cysteine 200, decreases the ADP-ribosyltransferase activity of the S1 subunit of pertussis toxin. J. Biol. Chem. 264 (1989) 6386-6390
41. Kharadia S.V., Huiatt T.W., Huang H.-Y., Peterson J.E., and Graves D.J. Effect of an arginine-specific ADP-ribosyltransferase inhibitor on differentiation of embryonic chick skeletal muscle cells in culture. Exp. Cell. Res. 201 (1992) 33-42
42. Klausner R.D., Donaldson J.G., and Lippincott-Schwartz J. Brefeldin A: Insights into the control of membrane traffic and organelle structure. J. Cell. Biol. 116 (1992) 1071-1080
43. Klebl B.M., Matsushita S., and Pette D. Localization of an arginine-specific mono-ADP-ribosyltransferase in skeletal muscle sarcolemma and transverse tubules. FEBS Lett. 342 (1994) 66-70
44. Koch F., Kashan A., and Thiele H.-G. The rat T-cell differentiation marker RT6.1 is more polymorphic than its alloantigenic counterpart RT6.2. Immunology 65 (1988) 259-265
45. Koch F., Haag F., Kashan A., and Thiele H.-G. Primary structure of rat RT6.2, a nonglycosylated phosphatidylinositol-linked surface marker of postthymic T cells. Proc. Natl. Acad. Sci. U.S.A. 87 (1990) 964-967
46. Koch T., and Ruger W. The ADP-ribosyltransferases (gpAlt) of bacteriophages T2, T4, and T6: Sequencing of the genes and comparison of their products. Virology 203 (1994) 294-298
47. Liu Y., and Kahn M.L. ADP-ribosylation of Rhizobium meliloti glutamine synthetase ID in vivo. J. Biol. Chem. 270 (1995) 1624-1628
48. Lobet Y., Cluff C.W., and Cieplak Jr. W. Effect of site-directed mutagenic alterations on ADP-ribosyltransferase activity of the A subunit of Escherichia cob heat-labile enterotoxin. Infect. Imnun. 59 (1991) 2870-2879
49. Ludden P.W. Reversible ADP-ribosylation as a mechanism of enzyme regulation in procaryotes. Mol. Cell. Biochem. 138 (1994) 123-129
50. Maehama T., Nishina H., and Katada T. ADP-ribosylarginine glycohydrolase catalyzing the release of ADP-ribose from the cholera toxin-modified α-subunits of GTP-binding proteins. J. Biochem. 116 (1994) 1134-1138
51. Marsischky G.T., Ikejima M., Suzuki H., Sugimura T., Esumi H., Miwa M., and Collier R.J. Directed mutagenesis of glutamic acid 988 of poly(ADP-ribose) polymerase. In: Poirier G.G., and Moreau P. (Eds). "ADP-ribosylation Reactions" (1992) 47-52
52. Matsuura R., Tanigawa Y., Tsuchiya M., Mishima K., Yoshimura Y., and Shimoyama M. ADP-ribosylation suppresses phosphorylation of the L-type pyruvate kinase. Biochem. Biophys. Acta 969 (1988) 57-65
53. Matsuyama S., and Tsuyama S. Mono-ADP-ribosylation in brain: Purification and characterization of ADP-ribosyltransferases affecting actin from rat brain. J. Neurochem. 57 (1991) 1380-1387
54. McDonald L.J., Wainschel L.A., Oppenheimer N.J., and Moss J. Amino acid-specific ADP-ribosylation: Structural characterization and chemical differentiation of ADP-ribose-cysteine adducts formed nonenzymatically and in a pertussis toxin-catalyzed reaction. Biochemistry 31 (1992) 11881-11887
55. McDonald L.J., and Moss J. Nitric oxide-independent, thiol-associated ADP-ribosylation inactivates aldehyde dehydrogenase. J. Biol. Chem. 268 (1993) 17878-17882
56. McDonald L.J., and Moss J. Stimulation by nitric oxide of a novel linkage of NAD to glyceraldehyde 3-phosphate dehydrogenase. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 6238-6241
57. McDonald L.J., and Moss J. Enzymatic and nonenzymatic ADP-ribosylation of cysteine. Mol. Cell. Biochem. 138 (1994) 221-226
58. McMahon K.K., Piron K.J., Ha V.T., and Fullerton A.T. Developmental and biochemical characteristics of the cardiac membrane-bound arginine-specific mono-ADP-ribosyltransferase. Biochem. J. 293 (1993) 789-793
59. Mishima K., Tsuchiya M., Tanigawa Y., Yoshimura Y., and Shimoyama M. DNA-dependent mono(ADP-ribosyl)ation of p33, an acceptor protein in hen liver nuclei. Eur. J. Biochem. 179 (1989) 267-273
60. Mishima K., Terashima M., Obara S., Yamada K., Imai K., and Shimoyama M. Arginine-specific ADP-ribosyltransferase and its acceptor protein p33 in chicken polymorpho-nuclear cells: Co-localization in the cell granules, partial characterization, and in situ mono(ADP-ribosyl)ation. J. Biochem. 110 (1991) 388-394
61. s). Biochem. J. 261 (1989) 841-845
62. Moss J., Stanley S.J., and Oppenheimer N.J. Substrate specificity and partial purification of a stereospecific NAD-and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes. J. Biol. Chem. 254 (1979) 8891-8894
63. Moss J., Stanley S.J., and Watkins P.A. Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes. J. Biol. Chem. 255 (1980) 5838-5840
64. Moss J., Stanley S.J., and Osborne Jr. J.C. Effect of self-association on activity of an ADP-ribosyltransferase from turkey erythrocytes. J. Biol. Chem. 256 (1981) 11452-11456
65. Moss J., Stanley S.J., and Osborne Jr. J.C. Activationof NAD:arginine ADP-ribosyltransferase by histone. J. Biol. Chem. 257 (1982) 1660-1663
66. Moss J., Osborne Jr. J.C., and Stanley S.J. Activation of an erythrocyte NAD:argin-ine ADP-ribosyltransferase by lysolecithin and nonionic and zwitterionic detergents. Biochemistry 23 (1984) 1353-1357
67. Moss J., Watkins P.A., Stanley S.J., Purnell M.R., and Kidwell W.R. Inactivation of glutamine synthetases by an NAD:arginine ADP-ribosyltransferase. J. Biol. Chem. 259 (1984) 5100-5104
68. Moss J., Jacobson M.K., and Stanley S.J. Reversibility of arginine-specific mono (ADP-ribosyl)ation: Identification in erythrocytes of an ADP-ribose-L-arginine cleavage enzyme. Proc. Natl. Acad. Sci. U.S.A. 82 (1985) 5603-5607
69. Moss J., Oppenheimer N.J., West Jr. R.E., and Stanley S.J. Amino acid specific ADP-ribosylation: Substrate specificity of an ADP-ribosylarginine hydrolase from turkey erythrocytes. Biochemistry 25 (1986) 5408-5414
70. Moss J., Tsai S.-C., Adamik R., Chen H.-C., and Stanley S.J. Purification and characterization of ADP-ribosylarginine hydrolase from turkey erythrocytes. Biochemistry 27 (1988) 5819-5823
71. Moss J., Stanley S.J., and Levine R.L. Inactivation of bacterial glutamine synthetase by ADP-ribosylation. J. Biol. Chem. 265 (1990) 21056-21060
72. Moss J., Stanley S.J., Nightingale M.S., Murtagh Jr. J.J., Monaco L., Mishima K., Chen H.-C., Williamson K.C., and Tsai S.-C. Molecular and Immunological characterization of ADP-ribosylarginine hydrolases. J. Biol. Chem. 267 (1992) 10481-10488
73. Moss J., Stanley S.J., Vaughan M., and Tsuji T. Interaction of ADP-ribosylation factor with Escherichia coli enterotoxin that contains an inactivating lysine 112 substitution. J. Biol. Chem. 268 (1993) 6383-6387
74. Moss J., and Stanley S.J. Histone-dependent and histone-independent forms of an ADP-ribosyltransferase from human and turkey erythrocytes. Proc. Natl. Acad. Sci. U.S.A. 78 (1981) 4809-4812
75. Moss J., and Stanley S.J. Amino acid-specific ADP-ribosylation. Identification of an arginine-dependent ADP-ribosyltransferase in rat liver. J. Biol. Chem. 256 (1981) 7830-7833
76. Moss J., and Vaughan M. Isolation of an avian erythrocyte protein possessing ADP-ribosyltransferase activity and capable of activating adenylate cyclase. Proc. Natl. Acad. Sci. U.S.A. 75 (1978) 3621-3624
77. Moss J., and Vaughan M. ADP-ribosylation of guanyl nucleotide-binding proteins by bacterial toxins. Adv. Enzymol. 61 (1988) 303-379
78. r guanine nucleotide-binding protein activators of cholera toxin and components of intracellular vesicular transport systems. Cell. Signal. 5 (1993) 367-379
79. Narumiya S., Sekine A., and Fujiwara M. Substrate for botulinum ADP-ribosyltransferase, Gb, has an amino acid sequence homologous to a putative rho gene product. J. Biol. Chem. 263 (1988) 17255-17257
80. Nemoto Y., Namba T., Kozaki S., and Narumiya S. Clostridium botulinum C3 ADP-ribosyltransferase gene. Cloning sequencing, and expression of a functional protein in Escherichia coli. J. Biol. Chem. 266 (1991) 19312-19319
81. Ness S.A., Marknell A., and Graf T. The v-myb oncogene product binds to and activates the promyelocyte-specific mim-1 gene. Cell 59 (1989) 1115-1125
82. Obara S., Yamada K., Yoshimura Y., and Shimoyama M. Evidence for the endogenous GTP-dependent ADP-ribosylation of the α-subunit of the stimulatory guanylnucleotide-binding protein concomitant with an increase in basal adenylyl cyclase activity in chicken spleen cell membrane. Eur. J. Biochem. 200 (1991) 75-80
83. Okazaki I.J., Zolkiewska A., Nightingale M.S., and Moss J. Immunological and structural conservation of mammalian skeletal muscle glycosylphosphatidylinositol-linked ADP-ribosyltransferases. Biochemistry 33 (1994) 12828-12836
84. I.J. Okazaki., H.-J. Kim., and G. McElvaney., J. Moss., (1996) Molecular characterization of a glycosylphosphatidylinositol-linked ADP-ribosyltransferase from lymphocytes. Submitted.
85. + with guanidines. J. Biol. Chem. 253 (1978) 4907-4910
86. Osborne Jr. J.C., Stanley S.J., and Moss J. Kinetic mechanisms of two NAD:arginine ADP-ribosyltransferases: The soluble, salt-stimulated transferase from turkey erythrocytes and choleragen, a toxin from Vibrio cholerae. Biochemistry 24 (1985) 5235-5240
87. + binding site of diphtheria toxin. J. Biol. Chem. 264 (1989) 12385-12388
88. Papini E., Santucci A., Schiavo G., Domenighini M., Neri P., Rappuoli R., and Montecucco R. Tyr-65 is photolabelled by 8-azido adenine and 8-azido-adenosine at the NAD binding site of diphtheria toxin. J. Biol. Chem. 266 (1991) 2494-2498
89. Pelham H.R.B. Multiple targets for brefeldin A. Cell 67 (1991) 449-451
90. Peterson J.E., Larew J.S.-A., and Graves D.J. Purification and partial characterization of arginine-specific ADP-ribosyltransferase from skeletal muscle microsomal membranes. J. Bio. Chem. 265 (1990) 17062-17069
91. Piron K.J., and McMahon K.K. Localization and partial characterization of ADP-ribosylation products in hearts from adult and neonatal rats. Biochem. J. 270 (1990) 591-597
92. Pizza M., Bartoloni A., Prugnola A., Silvestri S., and Rappuoli R. Subunit S1 of pertussis toxin: Mapping of the regions essential for ADP-ribosyltransferase activity. Proc. Natl. Acad. Sci. U.S.A. 85 (1988) 7521-7525
93. Pizza M., Domenighini M., Hoi W., Giannelli V., Fontana M.R., Giuliani M.M., Magag-noli C., Peppoloni S., Manetti R., and Rappuoli R. Probing the structure-activity relationship of Escherichia colt LT-A by site-directed mutagenesis. Mol. Microbiol. 14 (1994) 51-60
94. sα, by NAD and endogenous ADP-ribosyltransferase. J. Mol. Cell. Cardiol. 26 (1994) 251
95. +-dependent avian ADP-ribosyltransferase. Biochem. Biophys. Res. Commun. 184 (1992) 414-418
96. Rankin P.W., Jacobson E.L., Benjamin R.C., Moss J., and Jacobson M.K. Quantitative studies of inhibitors of ADP-ribosylation in vitro and in vivo. J. Biol. Chem. 264 (1989) 4312-4317
97. Rappuoli R., and Pizza M. Structure and evolutionary aspects of ADP-ribosylating toxins. In: Alouf J.E., and Freer J.H. (Eds). "Sourcebook of Bacterial Protein Toxins" (1991) 1-21
98. sα messenger RNA and protein in rat cerebral cortex. Proc. Natl. Acad. Sci. U.S.A. 86 (1989) 3906-3910
99. Scaife R.M., Wilson L., and Purich D.L. Microtubule protein ADP-ribosylation in vitro leads to assembly inhibition and rapid depolymerization. Biochemistry 31 (1992) 310-316
100. Schering B., Barmann M., Chhatwal G.S., Geipel U., and Aktories K. ADP-ribosylation of skeletal muscle and non-muscle actin by Clostridium perfringens iota toxin. Eur. J. Biochem. 171 (1988) 225-229
101. Schuman E.M., Meffert M.K., Schulman H., and Madison D.V. An ADP-ribosyltransferase as a potential target for nitric oxide action in hippocampal long-term potentiation. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 11958-11962
102. Sekine A., Fujiwara M., and Narumiya S. Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase. J. Biol. Chem. 264 (1989) 8602-8605
103. Simonin F., Poch O., Delarue M., and de Murcia G. Identification of potential active-site residues in the human poly(ADP-ribose) polymerase. J. Biol. Chem. 268 (1993) 8529-8535
104. Sixma T.K., Pronk S.E., Kalk K.H., Wartna E.S., vanZanten B.A.M., Witholt B., and Hol W.G.J. Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli. Nature (London) 351 (1991) 371-377
105. Smith K.P., Benjamin R.C., Moss J., and Jacobson M.K. Identification of enzymatic activities which process protein bound mono(ADP-ribose). Biochem. Biophys. Res. Commun. 126 (1985) 136-142
106. Soman G., Mickelson J.R., Louis C.F., and Graves D.J. NAD:guanidino group-specific mono-ADP-ribosyltransferase activity in skeletal muscle. Biochem. Biophys. Res. Commun. 120 (1984) 973-980
107. Soman G., Haregewoin A., Horn R.C., and Finberg R.W. Guanidine group specific ADP-ribosyltransferase in murine cells. Biochem. Biophys. Res. Commun. 176 (1991) 301-308
108. Song W.K., Wang W., Foster R.F., Bielser D.A., and Kaufamn S.J. H-36-alpha 7 is a novel integrin alpha chain that is developmentally regulated during skeletal myogenesis. J. Cell. Biol. 117 (1992) 643-657
109. Stein P.E., Boodhoo A., Armstrong G.D., Cockle S.A., Klein M.H., and Read R.J. The crystal structure of pertussis toxin. Structure 2 (1994) 45-57
110. Sternweis P.C., and Robishaw J.D. Isolation of two proteins with high affinity for guanine nucleotides from membrane of bovine brain. J. Biol. Chem. 259 (1984) 13806-13813
111. Takada T., Iida K., and Moss J. Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase. J. Biol. Chem. 268 (1993) 17837-17843
112. Takada T., Iida K., and Moss J. Expression of NAD glycohydrolase activity by rat mammary adenocarcinoma cells transformed with rat T cell alloantigen RT6.2. J. Biol. Chem. 269 (1994) 9420-9423
113. Takada T., Iida K., and Moss J. Conservation of a common motif in enzymes catalyzing ADP-ribose transfer. J. Biol. Chem. 270 (1995) 541-544
114. th International Symposium on ADP-ribosylation. DNA Repair, Signal Transduction". Abstract #56. Strasbourg-Bischenberg, France.
115. Tanigawa Y., Tsuchiya M., Imai Y., and Shimoyama M. Mono(ADP-ribosyl)ation of hen liver nuclear proteins suppresses phosphorylation. Biochem. Biophys. Res. Commun. 113 (1983) 135-141
116. Tanigawa Y., Tsuchiya M., Imai Y., and Shimoyama M. ADP-ribosylation regulates the phosphorylation of histones by the catalytic subunit of cyclic AMP-dependent protein kinase. FEBS Lett. 160 (1983) 217-220
117. Tanigawa Y., Tsuchiya M., Imai Y., and Shimoyama M. ADP-ribosyltransferase from hen liver nuclei. J. Biol. Chem. 259 (1984) 2022-2029
118. Tanuma S., Kawashima K., and Endo H. An NADxysteine ADP-ribosyltransferase is present in human erythrocytes. J. Biochem. 101 (1987) 821-824
119. i protein. J. Biol. Chem. 263 (1988) 5485-5489
120. i linkage. FEBS Lett. 261 (1990) 381-384
121. Terashima M., Mishima K., Yamada K., Tsuchiya M., Wakutani T., and Shimoyama M. ADP-ribosylation of actins by arginine-specific ADP-ribosyltransferase purified from chicken heterophils. Eur. J. Biochem. 204 (1992) 305-311
122. Thiele H.-G., Koch F., Hamann A., and Arndt R. Biochemical characterization of the T-cell alloantigen RT6.2. Immunology 59 (1986) 195-201
123. Tsai S.-C., Adamik R., Moss J., Vaughan M., Manne V., and Kung H.-F. Effects of phospholipids and ADP-ribosylation on GTP hydrolysis by Escherichia coli-synthesized Ha-ras-encoded p21. Proc. Natl. Acad. Sci. U.S.A. 82 (1985) 8310-8314
124. Tsai S.-C., Adamik R., Haun R.S., Moss J., and Vaughan M. Effects of brefeldin A and accessory proteins on association of ADP-ribosylation factors 1, 3, and 5 with Golgi. J. Biol. Chem. 268 (1993) 10820-10825
125. Tsuchiya M., Tanigawa Y., Ushiroyama T., Matsuura R., and Shimoyama M. ADP-ribosylation of phosphorylase kinase and block of phosphate incorporation into the enzyme. Eur. J. Biochem. 147 (1985) 33-40
126. Tsuchiya M., Hara N., Yamada K., Osago H., and Shimoyama M. Cloning and expression of cDNA for arginine-specific ADP-ribosykransferase from chicken bone marrow cells. J. Biol. Chem. 269 (1994) 27451-27457
127. Tsuji T., Inoue T., Miyama A., Okamoto K., Honda T., and Miwatani T. A single amino acid substitution in the A subunit of Escherichia coli enterotoxin results in a loss of its toxic activity. J. Biol. Chem. 265 (1990) 22520-22525
128. Tweten R.K., Barbieri J.T., and Collier R.J. Diphtheria toxin. Effect of substituting aspartic acid for glutamic acid 148 on ADP-ribosyltransferase activity. J. Biol. Chem. 260 (1985) 10392-10394
129. Ui M. Pertussis toxin as a valuable probe for G-protein involvement in signal transduc-tion. In: Moss J., and Vaughan M. (Eds). "ADP-ribosylating Toxins and G Proteins: Insights into Signal Transduction" (1990), American Society for Microbiology, Washington D.C. 45-77
130. Uroshiyama T., Tanigawa Y., Tsuchiya M., Matsurra R., Ueki M., Sugimoto O., and Shimoyama M. Amino acid sequence of histone H1 at the ADP-ribose-accepting site and ADP-ribose histone-H1 adduct as an inhibitor of cyclic-AMP-dependent phos-phorylation. Eur. J. Biochem. 151 (1985) 173-177
131. Vandekerckhove J., Schering B., Barmann M., and Aktories K. Clostridium per-fringens iota toxin ADP-ribosylates skeletal muscle actin in Arg-177. FEBS Lett. 225 (1987) 48-52
132. Vandekerckhove J., Schering B., Barmann M., and Aktories K. Botulinum C2 toxin ADP-ribosylates cytoplasmic β-γ-actin in arginine 177. J. Biol. Chem. 263 (1988) 696-700
133. Wang J., Nemoto E., Kots A.Y., Kaslow H.R., and Dennert G. Regulation of cytotoxic T cells by ecto-nicotinamide adenine dinucleotide (NAD) correlates with cell surface GPI-anchored/arginine ADP-ribosyltransferase. J. Immunol. 153 (1994) 4048-4058
134. Watkins P.A., and Moss J. Effects of nucleotides on activity of a purified ADP-ribosyltransferase from turkey erythrocytes. Arch. Biochem. Biophys. 216 (1982) 74-80
135. +:arginine ADP-ribosyltransferase from turkey erythrocytes. Biochem. J. 248 (1987) 749-754
136. Wegner A., and Aktories K. ADP-ribosylated actin caps the barbed ends of actin filaments. J. Biol. Chem. 263 (1988) 13739-13742
137. Welsh C.F., Moss J., and Vaughan M. ADP-ribosylation factors: A family of ~20-kDa guanine nucleotide-binding proteins that activate cholera toxin. Mol. Cell. Biochem. 138 (1994) 157-166
138. West Jr. R.E., and Moss J. Amino acid specific ADP-ribosylation: Specific NAD:argin-ine mono-ADP-ribosyltransferases associated with turkey erythrocyte nuclei and plasma membranes. Biochemistry 25 (1986) 8057-8062
139. Wick M.J., and Iglewski B.H. Pseudomonas aeruginosa exotoxin A. In: Moss J., and Vaughan M. (Eds). "ADP-ribosylating Toxins and G Proteins: Insights into Signal Transduction" (1990), American Society for Microbiology, Washington D.C. 31-43
140. Williamson K.C., and Moss J. Mono-ADP-ribosyltransferases and ADP-ribosylarginine hydrolases: A mono-ADP-ribosylation cycle in animal cells. In: Moss J., and Vaughan M. (Eds). "ADP-ribosylating Toxins and G Proteins: Insights into Signal Transduction" (1990), American Society for Microbiology, Washington D.C. 493-510
141. Wilson B.A., Blanke S.R., Reich K.A., and Collier R.J. Active-site mutations of diphtheria toxin. J. Biol. Chem. 269 (1994) 23296-23301
142. Wozniak D.J., Hsu L.-H., and Galloway D.R. His-426 of the Pseudomonas aeruginosa exotoxin A is required for ADP-ribosylation of elongation factor II. Proc. Natl. Acad. Sci. U.S.A. 85 (1988) 8880-8884
143. Xu Y., Barbancon-Finck V., and Barbieri J.T. Role of histidine 35 of the S1 subunit of pertussis toxin in the ADP-ribosylation of Transducin. J. Biol. Chem. 269 (1994) 9993-9999
144. Yamada K., Tsuchiya M., Mishima K., and Shimoyama M. p33, an endogenous target protein for arginine-specific ADP-ribosyltransferase in chicken polymorphonuclear leukocytes, is highly homologous to mim-1 protein (myb-induced myeloid protein-1). FEBS Lett. 311 (1992) 203-205
145. Yamada K., Tsuchiya M., Nishikori Y., and Shimoyama M. Automodification of arginine-specific ADP-ribosyltransferase purified from chicken peripheral heterophils and alteration of the transferase activity. Arch. Biochem. Biophys. 308 (1994) 31-36
146. Yost D.A., and Moss J. Amino acid-specific ADP-ribosylation. Evidence for two distinct NAD:arginine ADP-ribosyltransferases in turkey erythrocytes. J. Biol. Chem. 258 (1983) 4926-4929
147. Zolkiewska A., Nightingale M.S., and Moss J. Molecular characterization of NAD: arginine ADP-ribosyltransferase from rabbit skeletal muscle. Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 11352-11356
148. Zolkiewska A., and Moss J. Integrinα7 as substrate for a glycosylphosphatidylinositol-anchored ADP-ribosyltransferase on the surface of skeletal muscle cells. J. Biol. Chem. 268 (1993) 25273-25276
149. Zolkiewska A., and Moss J. Processing of ADP-ribosylated integrin α7 in skeletal muscle myotubes. J. Biol. Chem. 270 (1995) 9227-9233