Structural and biochemical studies identify tobacco SABP2 as a methyl salicylate esterase and implicate it in plant innate immunity

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 5, 2005, Pages 1773-1778

  Forouhar, Farhad ^a   Yang, Yue ^b   Kumar, Dhirendra ^c   Chen, Yang ^a   Fridman, Eyal ^b   Park, Sang Wook ^c   Chiang, Yiwen ^d   Acton, Thomas B ^d   Montelione, Gaetano T ^d   Pichersky, Eran ^b   Klessig, Daniel F ^c   Tong, Liang ^a  

^a Och Spine at New York Presbyterian Hospitals   (United States)

^b UNIVERSITY OF MICHIGAN   (United States)

^c United States Department of Agriculture Agricultural Research Service and Boyce Thompson Institute for Plant Research   (United States)

^d RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

Author keywords

hydrolase; Salicylic acid; Salicylic acid binding protein; Systemic acquired resistance

Indexed keywords

ASPARTIC ACID; BINDING PROTEIN; DRUG BINDING PROTEIN; ESTERASE; HISTIDINE; HYDROLASE; SALICYCLIC ACID BINDING PROTEIN 2; SALICYLIC ACID METHYL ESTER; SERINE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SUBSTRATE; HOST PATHOGEN INTERACTION; HUMORAL IMMUNITY; PLANT DEFENSE; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; CARBONIC ANHYDRASES; CATALASE; CRYSTALLOGRAPHY, X-RAY; ESTERASES; IMMUNITY, NATURAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PLANT PROTEINS; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; TOBACCO;

NICOTIANA TABACUM;

EID: 13444263252     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0409227102     Document Type: Article

References (39)

1. Dangl, J. L. & Jones, J. D. G. (2001) Nature 411, 826-833.
2. Holt, B. F., III, Hubert, D. A. & Dangl, J. L. (2003) Curr. Opin. Immunol. 15, 20-25.
3. Cohn, J., Sessa, G. & Martin, G. B. (2001) Curr. Opin. Immunol. 13, 55-62.
4. Hammond-Kosack, K. E. & Jones, J. D. G. (1996) Plant Cell 8, 1773-1791.
5. Dempsey, D., Shah, J. & Klessig, D. F. (1999) Crit. Rev. Plant Sci. 18, 547-575.
6. Dong, X. (2001) Curr. Opin. Plant Biol. 4, 309-314.
7. Glazebrook, J. (2001) Curr. Opin. Plant Biol. 4, 301-308.
8. Kunkel, B. N. & Brooks, D. M. (2002) Curr. Opin. Plant Biol. 5, 325-331.
9. van Camp, W., van Montagu, M. & Inze, D. (1998) Trends Plant Sci. 3, 330-334.
10. Draper, J. (1997) Trends Plant Sci. 2, 162-165.
11. Shirasu, K., Nakajima, H., Rajasekhar, V. K., Dixon, R. A. & Lamb, C. (1997) Plant Cell 9, 261-270.
12. Mur, L. A., Bi, Y. M., Darby, R. M., Firek, S. & Draper, J. (1997) Plant J. 12, 1113-1126.
13. Delaney, T. P., Uknes, S., Vernooij, B., Friedrich, L. B., Weymann, K. B., Negrotto, D., Gaffney, T., Gut-Rella, M., Kessmann, H., Ward, E., et al. (1994) Science 266, 1247-1250.
14. Gaffney, T., Friedrich, L. B., Vernooij, B., Negrotto, D., Nye, G., Uknes, S., Ward, E., Kessmann, H. & Ryals, J. (1993) Science 261, 754-756.
15. Shulaev, V., Silverman, P. & Raskin, I. (1997) Nature 385, 718-721.
16. Seskar, M., Shulaev, V. & Raskin, I. (1998) Plant Physiol. 116, 387-392.
17. Dudareva, N., Raguso, R. A., Wang, J., Ross, J. R. & Pichersky, E. (1998) Plant Physiol. 116, 599-604.
18. Enyedi, A. J., Yalpani, N., Silverman, P. & Raskin, I. (1992) Proc. Natl. Acad. Sci. USA 85, 2480-2484.
19. Malamy, J., Hennig, J. & Klessig, D. F. (1992) Plant Cell 4, 359-366.
20. Hennig, J., Malamy, J., Grynkiewicz, G., Indulski, J. & Klessig, D. F. (1993) Plant J. 4, 593-600.
21. Seo, S., Ishizuka, K. & Ohashi, Y. (1995) Plant Cell Physiol. 36, 447-453.
22. Ross, J. R., Nam, K. H., D'Auria, J. C. & Pichersky, E. (1999) Arch. Biochem. Biophys. 367, 9-16.
23. Chen, F., D'Auria, J. C., Tholl, D., Ross, J. R., Gershenzon, J., Noel, J. P. & Pichersky, E. (2003) Plant J. 36, 577-588.
24. Yalpani, N., Schulz, M., Davies, M. P. & Balke, N. E. (1992) Plant Physiol. 100, 457-463.
25. Du, H. & Klessig, D. F. (1997) Plant Physiol. 113, 1319-1327.
26. Kumar, D. & Klessig, D. F. (2003) Proc. Natl. Acad. Sci. USA 100, 16101-16106.
27. Ollis, D. L., Cheah, E., Cygler, M., Dijkstra, B., Frolow, F., Franken, S. M., Harel, M., Remington, S. J., Silman, I., Schrag, J., et al. (1992) Protein Eng. 5, 197-211.
28. Nardini, M. & Dijkstra, B. W. (1999) Curr. Opin. Struct. Biol. 9, 732-737.
29. Stuhlfelder, C., Mueller, M. J. & Warzecha, H. (2004) Eur. J. Biochem. 271, 2976-2983.
30. Dogru, E., Warzecha, H., Seibel, F., Haebel, S., Lottspeich, F. & Stockigt, J. (2000) Eur. J. Biochem. 267, 1397-1406.
31. Wagner, U. G., Hasslacher, M., Griengl, H., Schwab, H. & Kratky, C. (1996) Structure (London) 4, 811-822.
32. Otwinowski, Z. & Minor, W. (1997) Methods Enzymol. 276, 307-326.
33. Hendrickson, W. A. (1991) Science 254, 51-58.
34. Jogl, G., Tao, X., Xu, Y. & Tong, L. (2001) Acta Crystallogr. D 57, 1127-1134.
35. McRee, D. E. (1999) J. Struct. Biol. 125, 156-165.
36. Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J.-S., Kuszewski, J., Nilges, M., Pannu, N. S., et al. (1998) Acta Crystallogr. D 54, 905-921.
37. Gruber, K., Gartier, G., Krammer, B., Schwab, H. & Kratky, C. (2004) J. Biol. Chem. 279, 20501-20510.
38. Pichersky, E. & Gershenzon, J. (2002) Curr. Opin. Plant Biol. 5, 237-243.
39. Carson, M. (1987) J. Mol. Graphics 5, 103-106.