Molecular basis for the unique role of the AAA + chaperone ClpV in type VI protein secretion

Journal of Biological Chemistry

Volumn 286, Issue 34, 2011, Pages 30010-30021

  Pietrosiuk, Aleksandra ^a   Lenherr, Esther D ^a   Falk, Sebastian ^a   Bönemann, Gabriele ^a   Kopp, Jürgen ^a,b   Zentgraf, Hanswalter ^c   Sinning, Irmgard ^a   Mogk, Axel ^a  

^a UNIVERSITY OF HEIDELBERG   (Germany)

^b Excellenzcluster CellNetworks   (Germany)

^c GERMAN CANCER RESEARCH CENTER DKFZ   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ATPASES; BINDING AFFINITIES; CELLULAR PROCESS; MACROMOLECULAR COMPLEXES; MOLECULAR BASIS; MUTANT ANALYSIS; OLIGOMERIC STATE; PEPTIDE COMPLEX; PROTEIN SECRETION; RECOGNITION SITE; SUBSTRATE INTERACTION; SUBSTRATE SPECIFICITY; VIBRIO CHOLERAE; WEAK INTERACTIONS;

BINDING ENERGY; COMPLEXATION; CRYSTAL STRUCTURE; MACROMOLECULES; OLIGOMERS; PHYSIOLOGY; PROTEINS;

SUBSTRATES;

BACTERIAL PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN 100; MUTANT PROTEIN; OLIGOMER; PROTEIN AAA; PROTEIN CLPV; PROTEIN VIPA; PROTEIN VIPB; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; BACTERIAL VIRULENCE; BINDING AFFINITY; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME SPECIFICITY; HYDROPHOBICITY; MACROMOLECULE; MICROTUBULE ASSEMBLY; MOLECULAR BIOLOGY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN SECRETION; SEQUENCE HOMOLOGY; TYPE VI SECRETION SYSTEM; VIBRIO CHOLERAE;

ADENOSINE TRIPHOSPHATASES; BACTERIAL SECRETION SYSTEMS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; MOLECULAR CHAPERONES; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; VIBRIO CHOLERAE;

BACTERIA (MICROORGANISMS); VIBRIO CHOLERAE;

EID: 80051924474     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.253377     Document Type: Article

References (44)

1. Ogura, T., and Wilkinson, A. J. (2001) Genes Cells 6, 575-597
2. Hanson, P. I., and Whiteheart, S. W. (2005) Nat. Rev. Mol. Cell Biol. 6, 519-529
3. Sauer, R. T., Bolon, D. N., Burton, B. M., Burton, R. E., Flynn, J. M., Grant, R. A., Hersch, G. L., Joshi, S. A., Kenniston, J. A., Levchenko, I., Neher, S. B., Oakes, E. S., Siddiqui, S. M., Wah, D. A., and Baker, T. A. (2004) Cell 119, 9-18
4. Schmidt, R., Bukau, B., and Mogk, A. (2009) Res. Microbiol. 160, 629-636
5. Tyedmers, J., Mogk, A., and Bukau, B. (2010) Nat. Rev. Mol. Cell Biol. 11, 777-788
6. Kirstein, J., Schlothauer, T., Dougan, D. A., Lilie, H., Tischendorf, G., Mogk, A., Bukau, B., and Turgay, K. (2006) EMBO J. 25, 1481-1491
7. Dougan, D. A., Reid, B. G., Horwich, A. L., and Bukau, B. (2002) Mol. Cell 9, 673-683
8. Dougan, D. A., Weber-Ban, E., and Bukau, B. (2003) Mol. Cell 12, 373-380
9. Wah, D. A., Levchenko, I., Rieckhof, G. E., Bolon, D. N., Baker, T. A., and Sauer, R. T. (2003) Mol. Cell 12, 355-363
10. Wojtyra, U. A., Thibault, G., Tuite, A., and Houry, W. A. (2003) J. Biol. Chem. 278, 48981-48990
11. Bönemann, G., Pietrosiuk, A., Diemand, A., Zentgraf, H., and Mogk, A. (2009) EMBO J. 28, 315-325
12. Lee, S., Choi, J. M., and Tsai, F. T. (2007) Mol. Cell 25, 261-271
13. Effantin, G., Ishikawa, T., De Donatis, G. M., Maurizi, M. R., and Steven, A. C. (2010) Structure 18, 553-562
14. Mougous, J. D., Cuff, M. E., Raunser, S., Shen, A., Zhou, M., Gifford, C. A., Goodman, A. L., Joachimiak, G., Ordoñez, C. L., Lory, S., Walz, T., Joachimiak, A., and Mekalanos, J. J. (2006) Science 312, 1526-1530
15. Pukatzki, S., McAuley, S. B., and Miyata, S. T. (2009) Curr. Opin. Microbiol. 12, 11-17
16. Schwarz, S., Hood, R. D., and Mougous, J. D. (2010) Trends Microbiol. 18, 531-537
17. Leiman, P. G., Basler, M., Ramagopal, U. A., Bonanno, J. B., Sauder, J. M., Pukatzki, S., Burley, S. K., Almo, S. C., and Mekalanos, J. J. (2009) Proc. Natl. Acad. Sci. U.S.A. 106, 4154-4159
18. Bönemann, G., Pietrosiuk, A., and Mogk, A. (2010) Mol. Microbiol. 76, 815-821
19. Bange, G., Kümmerer, N., Engel, C., Bozkurt, G., Wild, K., and Sinning, I. (2010) Proc. Natl. Acad. Sci. U.S.A. 107, 11295-11300
20. Kabsch, W. (1993) J. Appl. Crystallogr. 26, 795-800
21. Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L. W., Kapral, G. J., Grosse-Kunstleve, R. W., McCoy, A. J., Moriarty, N. W., Oeffner, R., Read, R. J., Richardson, D. C., Richardson, J. S., Terwilliger, T. C., and Zwart, P. H. (2010) Acta Crystallogr. D Biol. Crystallogr. 66, 213-221
22. Emsley, P., Lohkamp, B., Scott, W. G., and Cowtan, K. (2010) Acta Crystallogr. D Biol. Crystallogr. 66, 486-501
23. Painter, J., and Merritt, E. A. (2006) Acta Crystallogr. D Biol. Crystallogr. 62, 439-450
24. Chen, V. B., Arendall, W. B., 3rd, Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., and Richardson, D. C. (2010) Acta Crystallogr. D Biol. Crystallogr. 66, 12-21
25. DeLano, W. L. (2008) The PyMOL Molecular Graphics System, DeLano Scientific LLC, Palo Alto, CA
26. Krissinel, E., and Henrick, K. (2007) J. Mol. Biol. 372, 774-797
27. Wallace, A. C., Laskowski, R. A., and Thornton, J. M. (1995) Protein Eng. 8, 127-134
28. Baker, N. A., Sept, D., Joseph, S., Holst, M. J., and McCammon, J. A. (2001) Proc. Natl. Acad. Sci. U.S.A. 98, 10037-10041
29. Holm, L., and Park, J. (2000) Bioinformatics 16, 566-567
30. Jones, D. T. (1999) J. Mol. Biol. 292, 195-202
31. Mogk, A., Schlieker, C., Strub, C., Rist, W., Weibezahn, J., and Bukau, B. (2003) J. Biol. Chem. 278, 17615-17624
32. Haslberger, T., Weibezahn, J., Zahn, R., Lee, S., Tsai, F. T., Bukau, B., and Mogk, A. (2007) Mol. Cell 25, 247-260
33. Schlieker, C., Weibezahn, J., Patzelt, H., Tessarz, P., Strub, C., Zeth, K., Erbse, A., Schneider-Mergener, J., Chin, J. W., Schultz, P. G., Bukau, B., and Mogk, A. (2004) Nat. Struct. Mol. Biol. 11, 607-615
34. Zeth, K., Ravelli, R. B., Paal, K., Cusack, S., Bukau, B., and Dougan, D. A. (2002) Nat. Struct. Biol. 9, 906-911
35. Guo, F., Esser, L., Singh, S. K., Maurizi, M. R., and Xia, D. (2002) J. Biol. Chem. 277, 46753-46762
36. Li, J., and Sha, B. (2003) Structure 11, 323-328
37. Kojetin, D. J., McLaughlin, P. D., Thompson, R. J., Dubnau, D., Prepiak, P., Rance, M., and Cavanagh, J. (2009) J. Mol. Biol. 387, 639-652
38. Pukatzki, S., Ma, A. T., Sturtevant, D., Krastins, B., Sarracino, D., Nelson, W. C., Heidelberg, J. F., and Mekalanos, J. J. (2006) Proc. Natl. Acad. Sci.U.S.A. 103, 1528-1533
39. Werbeck, N. D., Schlee, S., and Reinstein, J. (2008) J. Mol. Biol. 378, 178-190
40. Del Castillo, U., Fernández-Higuero, J. A., Pérez- Acebrón, S., Moro, F., and Muga, A. (2010) FEBS Lett. 584, 929-934
41. Schlieker, C., Zentgraf, H., Dersch, P., and Mogk, A. (2005) Biol. Chem. 386, 1115-1127
42. Wang, F., Mei, Z., Qi, Y., Yan, C., Hu, Q., Wang, J., and Shi, Y. (2011) Nature 471, 331-335
43. De Donatis, G. M., Singh, S. K., Viswanathan, S., and Maurizi, M. R. (2010) J. Biol. Chem. 285, 8771-8781
44. Hartman, J. J., and Vale, R. D. (1999) Science 286, 782-785