Mono(ADP-ribosyl)transferases and related enzymes in animal tissues: Emerging gene families

Advances in Experimental Medicine and Biology

Volumn 419, Issue , 1997, Pages 1-13

  Koch Nolte, Friedrich ^a   Haag, Friedrich ^a  

^a UNIVERSITY MEDICAL CENTER HAMBURG EPPENDORF   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROLASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE;

ADENOSINE DIPHOSPHATE RIBOSYLATION; CHOLERA; CONFERENCE PAPER; DIPHTHERIA; ENZYME ACTIVITY; ENZYME LOCALIZATION; ENZYME MECHANISM; MOLECULAR CLONING; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN MODIFICATION; PROTEIN PROCESSING; T LYMPHOCYTE;

EID: 0030990776     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4419-8632-0_1     Document Type: Conference Paper

References (63)

1. Honjo, T., Y. Nishizuka, O. Hayaishi and I. Kato. 1968. Diphtheria toxin/dependent adenosine diphosphate ribosylation of aminoacyl transferase II and inhibition of protein synthesis. J. Biol. Chem. 243: 3553-3555.
2. Passador, L. and W. Iglewski. 1994. ADP-ribosylating toxins. Methods Enzymol. 235: 617-631.
3. Reich, K. A. and G. K. Schoolnik. 1996. Halovibrin, screted from the light organ symbiont Vibrio fischeri, is a member of a new class of ADP-ribosyltransferases. J. Bacteriol. 178: 209-215.
4. Ludden, P. W. 1994. Reversible ADP-ribosylation as a mechanism of enzyme regulation in procaryotes. Mol. Cell. Biochem. 138: 123-129.
5. Koch, T. and W. Rüger. 1994. The ADP-ribosyltransferases (gpAlt) of bacteriophages T2, T4, and T6: sequencing of the genes and comparison of their products. Virology 203: 294-298.
6. Choe, S., M. J. Bennett, G. Fujii, P. M. Curmi, K. A. Kantardjieff, R. J. Collier and D. Eisenberg. 1992. The crystal structure of diphtheria toxin. Nature 357: 216-222.
7. Stein, P., A. Boodhoo, G. D. Armstrong, S. A. Cockle, M. H. Klein and R. J. Read. 1994. The crystal structure of pertussis toxin. Structure. Curr. Biol. 2: 45-57.
8. Domenighini, M., C. Magagnoli, M. Pizza and R. Rappuoli. 1994. Common features of the NAD-binding and catalytic site of ADP-ribosylating toxins. Mol. Microbiol. 14: 41-50.
9. Aktories, K. (ed.) 1991. ADP-ribosylating toxins. Springer Verlag, Berlin.
10. Aktories, K. and A. Wegner. 1992. Mechanisms of the cytopathic action of actin-ADP-ribosylating toxins. Mol. Microbiol. 6: 2905-8.
11. Althaus, F. R., H. Hilz and S. Shall. 1985. ADP-ribosylation of proteins. Springer Verlag, Berlin.
12. Kharadia, S. V., T. W. Huiatt, H. Y. Huang, J. E. Peterson and D. J. Graves. 1992. Effect of arginine-specific ADP-ribosyltransferase inhibitor on differentiation of embryonic chick skeletal muscle cells in culture. Exp. Cell Res. 201: 33-42.
13. McMahon, K. K., K. J. Piron, V. T. Ha and A. T. Fullerton. 1993. Developmental and biochemical characteristics of the cardiac membrane-bound arginine-specific mono-ADP-ribosyltransferase. Biochem. J. 293: 789-793.
14. Zolkiewska, A. and J. Moss. 1993. Integrin alpha 7 as substrate for a glycosylphosphatidylinositol-anchored ADP-ribosyltransferase on the surface of skeletal muscle cells. J. Biol. Chem. 268: 25273-25276.
15. Wang, J., E. Nemoto, A. Y. Kots, H. R. Kaslow and G. Dennert. 1994. Regulation of cytotoxic T cells by ecto-nicotinamide adenine dinucleotide (NAD) correlates with cell surface GPI-anchored/arginine ADP-ribosyltransferase. J. Immunol. 153: 4048-4058.
16. Hauschildt, S., P. Scheipers and W. G. Bessler. 1994. Lipopolysaccharide-induced change of ADP-ribosylation of a cytosolic protein in bone-marrow derived macrophages. Biochem. J. 297: 17-20.
17. Pellat, D. C., J. Wietzerbin and J. C. Drapier. 1994. Nicotinamide inhibits nitric oxide synthase mRNA induction in activated macrophages. Biochem. J. 297: 53-58.
18. Schuman, E. M., M. K. Meffert, H. Schulman and D. V. Madison. 1994. An ADP-ribosyltransferase as a potential target for nitric oxide action in hippocampal long-term potentiation. Proc. Natl. Acad. Sci. USA 91: 11958-11962.
19. lck associated protein. J. Immunol. 156: 2819-2827.
20. Godeau, F., D. Belin and S. S. Koide. 1984. Mono(adenosine diphoshpate ribosyl) transferase in Xenopus tissues. Direct demonstration by a zymographic localization in Sodium Dodecyl Sulfate-Polyacrylamide Gels. Anal. Biochem. 137: 287-296.
21. Brune, B., y. V. L. Molina and E. G. Lapetina. 1990. Agonist-induced ADP-ribosylation of a cytosolic protein in human platelets. Proc. Natl. Acad. Sci. USA 87: 3304-8.
22. Soman, G., A. Haregewoin, R. C. Hom and R. W. Finberg. 1991. Guanidine group specific ADP-ribosyltransferase in murine cells. Biochem. Biophys. Res. Commun. 176: 301-308.
23. Maehama, T. K., K. Takahashi, Y. Ohoka, T. Otsuka, M. Ui and T. Katada. 1991. Identification of a botulinum C3-like enzyme in bovine brain that catalyzes ADP-ribosylation of GTP-binding proteins. J. Biol. Chem. 266: 10062-10065.
24. Freiden, P. J., J. R. Gaut and L. M. Hendershot. 1992. Interconversion of three differentially modified and assembled forms of BiP. EMBO J. 11: 63-70.
25. Taniguchi, M., M. Tsuchiya and M. Shimoyama. 1993. Comparison of acceptor protein specificities on the formation of ADP-ribose acceptor adducts by arginine-specific ADP-ribosyltransferase from rabbit skeletal muscle sarcoplasmic reticulum with those of the enzyme from chicken peripheral polymorphonuclear cells. Biochim. Biophys. Acta 1161: 265-71.
26. Huang, H. Y., D. J. Graves, R. M. Robson and T. W. Huiatt. 1993. ADP-ribosylation of the intermediate filament protein desmin and inhibition of desmin assembly in vitro by muscle ADP-ribosyltransferase. Biochem. Biophys. Res. Commun. 197: 570-7.
27. Quist, E. E., D. L. Coyle, R. Vasan, N. Satumtira, E. L. Jacobson and M. K. Jacobson. 1994. Modification of cardiac membrane adenylate cyclase activity and Gs alpha by NAD and endogenous ADP-ribosyltransferase. J. Mol. Cell. Cardiol. 26: 251-260.
28. De Matteis, M., et al. 1994. Stimulation of endogenous ADP-ribosylation by brefeldin A. Proc. Natl. Acad. Sci .USA 91: 1114-8.
29. Zolkiewska, A., M. S. Nightingale and J. Moss. 1992. Molecular characterization of NAD:arginine ADP-ribosyltransferase from rabbit skeletal muscle. Proc. Natl. Acad. Sci. USA 89: 11352-11356.
30. Tsuchiya, M., N. Hara, K. Yamada, H. Osago and M. Shimoyama. 1994. Cloning and expression of cDNA for arginine-specific ADP-ribosyltransferase from chicken hone marrow cells. J. Biol. Chem. 269: 27451-27457.
31. Thiele, H. G., F. Koch, A. Hamann and R. Arndt. 1986. Biochemical characterization of the T-cell alloantigen RT-6.2. Immunol. 59: 195-201.
32. Koch, F., H. G. Thiele and M. G. Low. 1986. Release of the rat T cell alloantigen RT-6.2 from cell membranes by phosphatidylinositol-specific phospholipase C. J. Exp. Med. 164: 1338-1343.
33. Koch, F., F. Haag, A. Kashan and H. G. Thiele. 1990. Primary structure of rat RT6.2, a nonglycosylated phosphatidylinositol-linked surface marker of postthymic T cells. Proc. Natl. Acad. Sci. USA 87: 964-967.
34. Takada, T., K. Iida and J. Moss. 1994. Expression of NAD glycohydrolase activity by rat mammary adenocarcinoma cells transformed with rat T cell alloantigen RT6.2. J. Biol. Chem. 269: 9420-9423.
35. Haag, F., V. Andresen, S. Karsten, F. Koch-Nolte and H.-G. Thiele. 1995. Both allelic forms of the rat T cell differentiation marker RT6 display nicotinamide adenine dinucleotide (NAD)-glycohydrolase activity, yet only RT6.2 is capable of automodification upon incubation with NAD. Eur. J. Immunol. 25: 2355-2361.
36. Maehama, T., H. Nishina, S. Hoshino, Y. Kanaho and T. Katada. 1995. NAD+-dependent ADP-ribosylation of T lymphocyte alloantigen RT6.1 reversibly proceeding in intact rat lymphocytes. J. Biol. Chem. 270: 22747-22751.
37. Koch-Nolte, F., F. Haag, R. Kastelein and F. Bazan. 1996. Uncovered: The family relationship of a T cell membrane protein and bacterial toxins. Immunol. Today 17: 402-405.
38. Koch-Nolte, F., D. Petersen, S. Balasubramanian, F. Haag, D. Kahlke, T. Willer, R. Kastelein, F. Bazan and H. G. Thiele. 1996. Mouse T cell membrane proteins Rt6-1 and Rt6-2 are arginine/protein mono ADP-ribosyltransferases and share secondary structure motifs with ADP-ribosylating bacterial toxins. J. Biol. Chem. 271: 7686-7693.
39. Davis, T. and S. Shall. 1995. Sequence of a chicken erythroblast mono(ADP-ribosyl)transferase-encoding gene and its upstream region. Gene 164: 371-372.
40. Lévy, I., Y. Q. Wu, N. Roeckel, F. Bulle, A. Pawlak, S. Siegrist, M. G. Mattei and G. Guellaen. 1996. Human testis specifically expresses a homologue of the rodent T lymphocytes RT6 mRNA. FEBS Lett. 382: 276-280.
41. Koch-Nolte, F., F. Haag, R. Braren, M. Kühl, J. Hoovers, S. Balasubramanian, F. Bazan and H. G. Thiele. 1996. Two novel human members of an emerging mammalian gene family related to mono-ADP-ribosylating bacterial toxins. Genomics, in press.
42. Evans, R. J., V. Derkach and A. Surprenant. 1992. ATP mediates fast synaptic transmission in mammalian neurons. Nature 357: 503-505.
43. Valera, S., N. Hussy, R. J. Evans, N. Adami, R. A. North, A. Surprenant and G. Buell. 1994. A new class of ligand-gated ion channel defined by P2x receptor for extracellular ATP. Nature 371: 516-9.
44. Takada, T., K. Iida and J. Moss. 1995. Conservation of a common motif in enzymes catalyzing ADP-ribose transfer. Identification of domains in mammalian transferases. J. Biol. Chem. 270: 541-544.
45. DeMurcia, G. and J. MénissierDeMurcia. 1994. Trends Biochem. Sci. 19: 172-176.
46. Ruf, A., J. M. DeMurcia, G. M. DeMurcia and G. E. Schulz. 1996. Structure of the catalytic fragment of poly(ADP-ribose)polymerase from chicken. Proc. Natl. Acad. Sci. USA 93: 7481-7485.
47. Moss, J., S. J. Stanley, M. S. Nightingale, J. J. Murlagh, L. Monaco, K. Mishima, H. C. Chen, K. C. Williamson and S. C. Tsai. 1992. Molecular and immunological characterization of ADP-ribosylarginine hydrolases. J. Biol. Chem. 267: 10481-8.
48. Fitzmaurice, W. P., L. L. Saari, R. G. Lowery, P. W. Ludden and G. P. Roberts. 1989. Genes coding for the reversible ADP-ribosylation system of dinitrogenase reductase from Rhodospirillum rubrum. Mol. Gen. Genet. 218: 340-347.
49. Lee, H. C. and R. Aarhus. 1991. ADP-ribosyl cyclase: an enzyme that cyclizes NAD into a calcium-mobilizing metabolite. Cell. Regulation 2: 203.
50. Malavasi, F., A. Funaro, S. Roggero, A. Horenstein, L. Calosso and K. Mehta. 1994. Human CD38: a glycoprotein in search of a function. Immunol Today 15: 95-97.
51. Howard, M., J. C. Grimaldi, J. F. Bazan, F. E. Lund, A. L. Santos, R. M. Parkhouse, T. F. Walseth and H. C. Lee. 1993. Formation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38. Science 262: 1056-1059.
52. Grimaldi, J. C., S. Balasubramanian, N. H. Kabra, A. Shanafelt, J. F. Bazan, G. Zurawski and M. C. Howard. 1995. CD38-mediated ribosylation of proteins. J. Immunol. 155: 811-817.
53. Greiner, D. L., E. S. Handler, K. Nakano, J. P. Mordes and A. A. Rossini. 1986. Absence of the RT-6 T cell subset in diabetes-prone BB/W rats. J. Immunol. 136: 148-151.
54. Koch-Nolte, F., J. Klein, C. Hollmann, M. Kühl, F. Haag, H. R. Gaskins, E. H. Leiter and H. G. Thiele. 1995. Defects in the structure and expression of the genes for the T cell marker Rt6 in NZW and (NZB x NZW)F1 mice. Int. Immunol. 7: 883-890.
55. Burstein, D., J. P. Mordes, D. L. Greiner, D. Stein, N. Nakamura, E. S. Handler and A. A. Rossini. 1989. Prevention of diabetes in BB/Wor rat by single transfusion of spleen cells. Parameters that affect degree of protection. Diabetes 38: 24-30.
56. McKeever, U., J. P. Mordes, D. L. Greiner, M. C. Appel, J. Rozing, E. S. Handler and A. A. Rossini. 1990. Adoptive transfer of autoimmune diabetes and thyroiditis to athymic rats. Proc .Natl. Acad. Sci. USA 87: 7618-22.
57. Fowell, D. and D. Mason. 1993. Evidence that the T cell repertoire of normal rats contains cells with the potential to cause diabetes. Characterization of the CD4+ T cell subset that inhibits this autoimmune potential. J. Exp. Med. 177: 627-36.
58. Greiner, D. L., J. P. Mordes, E. S. Handler, M. Angelillo, N. Nakamura and A. A. Rossini. 1987. Depletion of RT6.1+ T lymphocytes induces diabetes in resistant biobreeding/Worcester (BB/W) rats. J. Exp. Med. 166: 461-475.
59. Drake, C. G., S. J. Rozzo, H. F. Hirschfeld, N. P. Smarnworawong, E. Palmer and B. L. Kotzin. 1995. Analysis of the New Zealand Black contribution to lupus-like renal disease. Multiple genes that operate in a threshold manner. J. Immunol. 154: 2441-2447.
60. Williamson, K. C. and J. Moss. 1990. Mono-ADP ribosyltransferases and ADP-ribosylarginine hydrolases: a mono-ADP-ribosylation cycle in animal cells. In: ADP-ribosylating bacterial toxins and G-proteins. Insights into signal transduction. (J. Moss and M. Vaughan, eds.). American Society for Microbiology, Washington D.C.
61. Okuyama, T., S. Sato, X. L. Zhu, A. Waheed and W. S. Sly. 1992. Human carbonic anhydrase IV: cDNA cloning, sequence comparison, and expression in COS cell membranes. Proc. Natl. Acad. Sci. USA 89: 1315-1319.
62. Haag, F., F. Koch-Nolte, M. Kühl, S. Lorenzen and H. G. Thiele. 1994. Premature stop codons inactivate the RT6 genes of the human and chimpanzee species. J. Mol. Biol. 243: 537-546.
63. Hollmann, C., F. Haag, M. Schlott, A. Damaske, H. Bertuleit, M. Matthes, M. Kühl, H. G. Thiele and F. Koch-Nolte. 1996. Molecular characterization of mouse T-cell ecto-ADP-ribosyltransferase Rt6: cloning of a second functional gene and identification of the Rt6 gene products. Mol. Immunol. 33: 807-817.