2′-5′ Oligoadenylate synthetase shares active site architecture with the archaeal CCA-adding enzyme

Cellular and Molecular Life Sciences

Volumn 65, Issue 16, 2008, Pages 2613-2620

  Torralba, S ^a   Sojat, J ^a   Hartmann, R ^a  

^a AARHUS UNIVERSITY   (Denmark)

Author keywords

Archaeal CCA adding enzyme; Interferon; Oligoadenylate synthetase; Poly adenosine polymerase; RNA metabolism

Indexed keywords

2 5 OLIGOADENYLATE SYNTHETASE; AMINO ACID; ARCHAEAL PROTEIN; NUCLEOTIDYLTRANSFERASE; POLYADENOSINE POLYMERASE; SYNTHETASE; UNCLASSIFIED DRUG; 2',5' OLIGOADENYLATE SYNTHETASE; ADENOSINE TRIPHOSPHATE; MUTANT PROTEIN; RNA POLYMERASE; TRANSFER RIBONUCLEIC ACID NUCLEOTIDYLTRANSFERASE;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME STRUCTURE; MOLECULAR EVOLUTION; MUTAGENESIS; NONHUMAN; NUCLEOTIDE SEQUENCE; STRUCTURAL HOMOLOGY; AMINO ACID SEQUENCE; ANIMAL; ARCHAEOGLOBUS FULGIDUS; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; DNA TEMPLATE; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; SEQUENCE ALIGNMENT; SWINE;

ARCHAEA; METAZOA;

2',5'-OLIGOADENYLATE SYNTHETASE; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; ARCHAEOGLOBUS FULGIDUS; BINDING SITES; EVOLUTION, MOLECULAR; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; MUTATION; RNA NUCLEOTIDYLTRANSFERASES; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY, PROTEIN; SWINE; TEMPLATES, GENETIC;

EID: 50249139546     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-008-8164-5     Document Type: Article

References (36)

1. Justesen, J., Hartmann, R. and Kjeldgaard, N. O. (2000) Gene structure and function of the 2′-5′-oligoadenylate synthetase family. Cell. Mol. Life Sci. 57, 1593-612.
2. Rebouillat, D. and Hovanessian, A.G. (1999) The human 2′,5′-oligoadenylate synthetase family: Interferon-induced proteins with unique enzymatic properties. J. Interferon Cytokine Res. 19, 295-308.
3. Silverman, R. H. (2007) A scientific journey through the 2-5A/RNase L system. Cytokine Growth Factor Rev. 18, 381-8.
4. Cayley, P. J., White, R. F., Antoniw, J. F., Walesby, N. J. and Kerr, I. M. (1982) Distribution of the ppp(A2′p)nA-binding protein and interferon-related enzymes in animals, plants, and lower organisms. Biochem. Biophys. Res. Commun. 108, 1243-50.
5. Holm, L. and Sander, C. (1995) DNA polymerase beta belongs to an ancient nucleotidyltransferase superfamily. Trends Biochem. Sci. 20, 345-7.
6. Sarkar, S. N., Ghosh, A., Wang, H. W., Sung, S. S. and Sen, G. C. (1999) The nature of the catalytic domain of 2′-5′-oligoadenylate synthetases. J. Biol. Chem. 274, 25535-42.
7. Hartmann, R., Justesen, J., Sarkar, S. N., Sen, G. C. and Yee, V. C. (2003) Crystal structure of the 2′-specific and double-stranded RNA-activated interferon-induced antiviral protein 2′-5′- oligoadenylate synthetase. Mol. Cell 12, 1173-85.
8. Cho, H. D., Verlinde, C. L. and Weiner, A. M. (2005) Archaeal CCA-adding enzymes: Central role of a highly conserved beta-turn motif in RNA polymerization without translocation. J. Biol. Chem. 280, 9555-66.
9. Martin, G., Jeno, P. and Keller, W. (1999) Mapping of ATP binding regions in poly(A) polymerases by photoaffinity labeling and by mutational analysis identifies a domain conserved in many nucleotidyltransferases. Protein Sci. 8, 2380-91.
10. Steitz, T. A. (1998) A mechanism for all polymerases. Nature 391, 231-2.
11. Hovanessian, A. G. and Justesen, J. (2007) The human 2′-5′ oligoadenylate synthetase family: Unique interferon-inducible enzymes catalyzing 2′-5′ instead of 3′-5′ phosphodiester bond formation. Biochimie 89, 779-88.
12. Hovanessian, A. G., Laurent, A. G., Chebath, J., Galabru, J., Robert, N. and Svab, J. (1987) Identification of 69-kd and 100-kd forms of 2-5A synthetase in interferon-treated human cells by specific monoclonal antibodies. EMBO J. 6, 1273-80.
13. Hartmann, R., Olsen, H. S., Widder, S., Jorgensen, R. and Justesen, J. (1998) p59OASL, a 2′-5′ oligoadenylate synthetase like protein: A novel human gene related to the 2′-5′ oligoadenylate synthetase family. Nucleic Acids Res. 26, 4121-8.
14. Rebouillat, D., Marie, I. and Hovanessian, A. G. (1998) Molecular cloning and characterization of two related and interferon-induced 56-kDa and 30-kDa proteins highly similar to 2′-5′ oligoadenylate synthetase. Eur. J. Biochem. 257, 319-30.
15. Kumar, S., Mitnik, C., Valente, G. and Floyd-Smith, G. (2000) Expansion and molecular evolution of the interferon-induced 2′-5′ oligoadenylate synthetase gene family. Mol. Biol. Evol. 17, 738-50.
16. Jones, T. A., Zou, J. Y., Cowan, S. W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-9.
17. Justesen, J., Ferbus, D. and Thang, M. N. (1980) 2′5′ oligoadenylate synthetase, an interferon induced enzyme: Direct assay methods for the products, 2′5′ oligoadenylates and 2′5′ co-oligonucleotides. Nucleic Acids Res. 8, 3073-85.
18. Martin, G., Keller, W. and Doublie, S. (2000) Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP. EMBO J. 19, 4193-203.
19. Bard, J., Zhelkovsky, A. M., Helmling, S., Earnest, T. N., Moore, C. L. and Bohm, A. (2000) Structure of yeast poly(A) polymerase alone and in complex with 3′-dATP. Science 289, 1346-9.
20. Balbo, P. B. and Bohm, A. (2007) Mechanism of poly(A) polymerase: Structure of the enzyme-MgATP-RNA ternary complex and kinetic analysis. Structure 15, 1117-31.
21. Xiong, Y. and Steitz, T. A. (2004) Mechanism of transfer RNA maturation by CCA-adding enzyme without using an oligonucleotide template. Nature 430, 640-5.
22. Tomita, K., Fukai, S., Ishitani, R., Ueda, T., Takeuchi, N., Vassylyev, D. G. and Nureki, O. (2004) Structural basis for template-independent RNA polymerization. Nature 430, 700-4.
23. Emsley, P. and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-32.
24. Sarkar, S. N., Miyagi, M., Crabb, J. W. and Sen, G. C. (2002) Identification of the substrate-binding sites of 2′-5′- oligoadenylate synthetase. J. Biol. Chem. 277, 24321-30.
25. Yue, D., Weiner, A. M. and Maizels, N. (1998) The CCA-adding enzyme has a single active site. J. Biol. Chem. 273, 29693-700.
26. Okabe, M., Tomita, K., Ishitani, R., Ishii, R., Takeuchi, N., Arisaka, F., Nureki, O. and Yokoyama, S. (2003) Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding enzyme structure. EMBO J. 22, 5918-27.
27. Steitz, T. A. (1999) DNA polymerases: Structural diversity and common mechanisms. J. Biol. Chem. 274, 17395-8.
28. Tomita, K., Ishitani, R., Fukai, S. and Nureki, O. (2006) Complete crystallographic analysis of the dynamics of CCA sequence addition. Nature 443, 956-60.
29. Yue, D., Maizels, N. and Weiner, A. M. (1996) CCA-adding enzymes and poly(A) polymerases are all members of the same nucleotidyltransferase superfamily: Characterization of the CCA-adding enzyme from the archaeal hyperthermophile Sulfolobus shibatae. RNA 2, 895-908.
30. Deng, J., Ernst, N. L., Turley, S., Stuart, K. D. and Hol, W. G. (2005) Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei. EMBO J. 24, 4007-17.
31. Chen, C. C., Simard, M. J., Tabara, H., Brownell, D. R., McCollough, J. A. and Mello, C. C. (2005) A member of the polymerase beta nucleotidyltransferase superfamily is required for RNA interference in C. elegans. Curr. Biol. 15, 378-83.
32. Delarue, M., Boule, J. B., Lescar, J., Expert-Bezancon, N., Jourdan, N., Sukumar, N., Rougeon, F. and Papanicolaou, C. (2002) Crystal structures of a template-independent DNA polymerase: Murine terminal deoxynucleotidyltransferase. EMBO J. 21, 427-39.
33. Stark, G. R., Dower, W. J., Schimke, R. T., Brown, R. E. and Kerr, I. M. (1979) 2-5A synthetase: Assay, distribution and variation with growth or hormone status. Nature 278, 471-3.
34. Kuusksalu, A., Pihlak, A., Muller, W. E. and Kelve, M. (1995) The (2′-5′)oligoadenylate synthetase is present in the lowest multicellular organisms, the marine sponges. Demonstration of the existence and identification of its reaction products. Eur. J. Biochem. 232, 351-7.
35. Wiens, M., Koziol, C., Hassanein, H. M., Muller, I. M. and Muller, W. E. (1999) A homolog of the putative tumor suppressor QM in the sponge Suberites domuncula: Downregulation during the transition from immortal to mortal (apoptotic) cells. Tissue Cell 31, 163-9.
36. Venkatesh, B., Kirkness, E. F., Loh, Y. H., Halpern, A. L., Lee, A. P., Johnson, J., Dandona, N., Viswanathan, L. D., Tay, A., Venter, J. C., Strausberg, R. L. and Brenner, S. (2007) Survey sequencing and comparative analysis of the Elephant Shark (Callorhinchus milii) genome. PLoS Biol 5, e101.