Structure function analysis of an ADP-ribosyltransferase type III effector and its RNA-binding target in plant immunity

Journal of Biological Chemistry

Volumn 286, Issue 50, 2011, Pages 43272-43281

  Jeong, Byeong Ryool ^a   Lin, Yan ^b   Joe, Anna ^c   Guo, Ming ^a   Korneli, Christin ^d   Yang, Huirong ^b   Wang, Ping ^b   Yu, Min ^b   Cerny, Ronald L ^a   Staiger, Dorothee ^d   Alfano, James R ^a   Xu, Yanhui ^b  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

^b FUDAN UNIVERSITY   (China)

^c UNIVERSITY OF NEBRASKA   (United States)

^d BIELEFELD UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADP-RIBOSYLTRANSFERASE; ARABIDOPSIS THALIANA; ENZYMATIC ACTIVITIES; GLYCINE-RICH RNA-BINDING PROTEINS; IMMUNE RESPONSE; IN-VITRO; IN-VIVO; PLANT CELLS; PROTEIN SECRETION SYSTEM; PSEUDOMONAS SYRINGAE; RNA BINDING; RNA-BINDING PROTEIN; SITE DIRECTED MUTAGENESIS; STRUCTURE-FUNCTION ANALYSIS; SUBSTRATE RECOGNITION;

AMINO ACIDS; ENZYME ACTIVITY; PLANT CELL CULTURE; PLANTS (BOTANY); PROTEINS; RNA;

CRYSTAL STRUCTURE;

ARGININE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEIN GRP7; PROTEIN HOPU1; RNA BINDING PROTEIN; UNCLASSIFIED DRUG;

ARABIDOPSIS; ARTICLE; BACTERIAL STRAIN; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME ANALYSIS; ESCHERICHIA COLI; IMMUNE RESPONSE; NONHUMAN; PLANT CELL; PLANT IMMUNITY; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PURIFICATION; PSEUDOMONAS SYRINGAE; RNA BINDING; SITE DIRECTED MUTAGENESIS; TYPE III SECRETION SYSTEM;

ADP RIBOSE TRANSFERASES; ARABIDOPSIS; ARABIDOPSIS PROTEINS; PLANT IMMUNITY; PLANT PROTEINS; PLANTS, GENETICALLY MODIFIED; PROTEIN BINDING; RNA, PLANT; RNA-BINDING PROTEINS;

EID: 83355169694     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.290122     Document Type: Article

References (66)

1. Büttner, D., and He, S. Y. (2009) Plant Physiol. 150, 1656-1664
2. Alfano, J. R., and Collmer, A. (2004) Annu. Rev. Phytopathol. 42, 385-414
3. Hann, D. R., Gimenez-Ibanez, S., and Rathjen, J. P. (2010) Curr. Opin. Plant Biol. 13, 388-393
4. Block, A., and Alfano, J. R. (2011) Curr. Opin. Microbiol. 14, 39-46
5. Boller, T., and Felix, G. (2009) Annu. Rev. Plant Biol. 60, 379-406
6. Jones, J. D., and Dangl, J. L. (2006) Nature 444, 323-329
7. Tsuda, K., and Katagiri, F. (2010) Curr. Opin. Plant Biol. 13, 459-465
8. Lindeberg, M., Cartinhour, S., Myers, C. R., Schechter, L. M., Schneider, D. J., and Collmer, A. (2006) Mol. Plant Microbe Interact. 19, 1151-1158
9. Guo, M., Tian, F., Wamboldt, Y., and Alfano, J. R. (2009) Mol. Plant Microbe Interact. 22, 1069-1080
10. Rosebrock, T. R., Zeng, L., Brady, J. J., Abramovitch, R. B., Xiao, F., and Martin, G. B. (2007) Nature 448, 370-374
11. Xiang, T., Zong, N., Zou, Y., Wu, Y., Zhang, J., Xing, W., Li, Y., Tang, X., Zhu, L., Chai, J., and Zhou, J. M. (2008) Curr. Biol. 18, 74-80
12. Shan, L., He, P., Li, J., Heese, A., Peck, S. C., Nürnberger, T., Martin, G. B., and Sheen, J. (2008) Cell Host Microbe 4, 17-27
13. Göhre, V., Spallek, T., Häweker, H., Mersmann, S., Mentzel, T., Boller, T., de Torres, M., Mansfield, J. W., and Robatzek, S. (2008) Curr. Biol. 18, 1824-1832
14. Gimenez-Ibanez, S., Hann, D. R., Ntoukakis, V., Petutschnig, E., Lipka, V., and Rathjen, J. P. (2009) Curr. Biol. 19, 423-429
15. Wang, Y., Li, J., Hou, S., Wang, X., Li, Y., Ren, D., Chen, S., Tang, X., and Zhou, J. M. (2010) Plant Cell 22, 2033-2044
16. Zhang, J., Shao, F., Li, Y., Cui, H., Chen, L., Li, H., Zou, Y., Long, C., Lan, L., Chai, J., Chen, S., Tang, X., and Zhou, J. M. (2007) Cell Host Microbe 1, 175-185
17. Nomura, K., Debroy, S., Lee, Y. H., Pumplin, N., Jones, J., and He, S. Y. (2006) Science 313, 220-223
18. Fu, Z. Q., Guo, M., Jeong, B. R., Tian, F., Elthon, T. E., Cerny, R. L., Staiger, D., and Alfano, J. R. (2007) Nature 447, 284-288
19. Block, A., Guo, M., Li, G., Elowsky, C., Clemente, T. E., and Alfano, J. R. (2010) Cell. Microbiol. 12, 318-330
20. Jelenska, J., van Hal, J. A., and Greenberg, J. T. (2010) Proc. Natl. Acad. Sci. U.S.A. 107, 13177-13182
21. Fieldhouse, R. J., and Merrill, A. R. (2008) Trends Biochem. Sci. 33, 546-556
22. Deng, Q., and Barbieri, J. T. (2008) Annu. Rev. Microbiol. 62, 271-288
23. Aktories, K., Wilde, C., and Vogelsgesang, M. (2004) Rev. Physiol. Biochem. Pharmacol. 152, 1-22
24. Holbourn, K. P., Shone, C. C., and Acharya, K. R. (2006) FEBS J. 273, 4579-4593
25. Barbieri, J. T., and Burns, D. L. (2003) in Bacterial Protein Toxins (Burns, D. L., Barbieri, J. T., Iglewski, B. H., and Rappuoli, R., eds) pp. 215-228, American Society for Microbiology Press, Washinton, D. C.
26. Hottiger, M. O., Hassa, P. O., Lüscher, B., Schüler, H., and Koch-Nolte, F. (2010) Trends Biochem. Sci. 35, 208-219
27. Mueller-Dieckmann, C., Ritter, H., Haag, F., Koch-Nolte, F., and Schulz, G. E. (2002) J. Mol. Biol. 322, 687-696
28. Okazaki, I. J., and Moss, J. (1996) Rev. Physiol. Biochem. Pharmacol. 129, 51-104
29. Ménétrey, J., Flatau, G., Boquet, P., Ménez, A., and Stura, E. A. (2008) Protein Sci. 17, 878-886
30. Schmidt, F., Marnef, A., Cheung, M. K., Wilson, I., Hancock, J., Staiger, D., and Ladomery, M. (2010) Mol. Biol. Rep. 37, 839-845
31. Kim, J. S., Jung, H. J., Lee, H. J., Kim, K. A., Goh, C. H., Woo, Y., Oh, S. H., Han, Y. S., and Kang, H. (2008) Plant J. 55, 455-466
32. Streitner, C., Danisman, S., Wehrle, F., Schöning, J. C., Alfano, J. R., and Staiger, D. (2008) Plant J. 56, 239-250
33. Sambrook, J., and Russell, D. W. (2001) Molecular Cloning: A Laboratory Manual, 3rd Ed., Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
34. King, E. O., Ward, M. K., and Raney, D. E. (1954) J. Lab. Clin. Med. 44, 301-307
35. Bechtold, N., Ellis, J., and Pelletier, G. (1993) C. R. Acad. Sci. Paris 316, 1194-1199
36. Lin, Y., Wang, P., Yang, H., and Xu, Y. (2010) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66, 932-934
37. Terwilliger, T. C., Adams, P. D., Read, R. J., McCoy, A. J., Moriarty, N. W., Grosse-Kunstleve, R. W., Afonine, P. V., Zwart, P. H., and Hung, L. W. (2009) Acta Crystallogr. D Biol. Crystallogr. 65, 582-601
38. Emsley, P., and Cowtan, K. (2004) Acta Crystallogr. D Biol. Crystallogr 60, 2126-2132
39. Laskowski, R. A., Moss, D. S., and Thornton, J. M. (1993) J. Mol. Biol. 231, 1049-1067
40. Holm, L., Kääriäinen, S., Rosenström, P., and Schenkel, A. (2008) Bioinformatics 24, 2780-2781
41. Arnold, K., Bordoli, L., Kopp, J., and Schwede, T. (2006) Bioinformatics 22, 195-201
42. Arnold, K., Kiefer, F., Kopp, J., Battey, J. N., Podvinec, M., Westbrook, J. D., Berman, H. M., Bordoli, L., and Schwede, T. (2009) J. Struct. Funct. Genomics 10, 1-8
43. Chen, R., Li, L., and Weng, Z. (2003) Proteins 52, 80-87
44. Kayser, J. P., Vallet, J. L., and Cerny, R. L. (2004) J. Biomol. Tech. 15, 285-295
45. Schöning, J. C., Streitner, C., Page, D. R., Hennig, S., Uchida, K., Wolf, E., Furuya, M., and Staiger, D. (2007) Plant J. 52, 1119-1130
46. Asai, S., Ohta, K., and Yoshioka, H. (2008) Plant Cell 20, 1390-1406
47. Mavrodi, D. V., Joe, A., Mavrodi, O. V., Hassan, K. A., Weller, D. M., Paulsen, I. T., Loper, J. E., Alfano, J. R., and Thomashow, L. S. (2011) J. Bacteriol. 193, 177-189
48. Abramoff, M. D., Magelhaes, P. J., and Ram, S. J. (2004) Biophoton. Int. 11, 36-42
49. Yuan, J., and He, S. Y. (1996) J. Bacteriol. 178, 6399-6402
50. Crabill, E., Joe, A., Block, A., van Rooyen, J. M., and Alfano, J. R. (2010) Plant Physiol. 154, 233-244
51. Espinosa, A., Guo, M., Tam, V. C., Fu, Z. Q., and Alfano, J. R. (2003) Mol. Microbiol. 49, 377-387
52. Rost, B., Yachdav, G., and Liu, J. (2004) Nucleic Acids Res. 32, W321-326
53. Rao, S. T., and Rossmann, M. G. (1973) J. Mol. Biol. 76, 241-256
54. Han, S., and Tainer, J. A. (2002) Int. J. Med. Microbiol. 291, 523-529
55. Maris, C., Dominguez, C., and Allain, F. H. (2005) FEBS J. 272, 2118-2131
56. Tsuge, H., Nagahama, M., Oda, M., Iwamoto, S., Utsunomiya, H., Marquez, V. E., Katunuma, N., Nishizawa, M., and Sakurai, J. (2008) Proc. Natl. Acad. Sci. U.S.A. 105, 7399-7404
57. Wilton, M., Subramaniam, R., Elmore, J., Felsensteiner, C., Coaker, G., and Desveaux, D. (2010) Proc. Natl. Acad. Sci. U.S.A. 107, 2349-2354
58. Singer, A. U., Desveaux, D., Betts, L., Chang, J. H., Nimchuk, Z., Grant, S. R., Dangl, J. L., and Sondek, J. (2004) Structure 12, 1669-1681
59. Ding, J., Hayashi, M. K., Zhang, Y., Manche, L., Krainer, A. R., and Xu, R. M. (1999) Genes Dev. 13, 1102-1115
60. Nagai, K., Oubridge, C., Jessen, T. H., Li, J., and Evans, P. R. (1990) Nature 348, 515-520
61. Lee, A. L., Volkman, B. F., Robertson, S. A., Rudner, D. Z., Barbash, D. A., Cline, T. W., Kanaar, R., Rio, D. C., and Wemmer, D. E. (1997) Biochemistry 36, 14306-14317
62. Galán, J. E. (2009) Cell Host Microbe 5, 571-579
63. Cléry, A., Blatter, M., and Allain, F. H. (2008) Curr. Opin. Struct. Biol. 18, 290-298
64. Ludden, P. W., and Roberts, G. P. (1989) Curr. Top. Cell Regul. 30, 23-56
65. Heintzen, C., Nater, M., Apel, K., and Staiger, D. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 8515-8520
66. Streitner, C., Hennig, L., Korneli, C., and Staiger, D. (2010) BMC Plant Biol. 10, 221-234