A disulfide bridge network within the soluble periplasmic domain determines structure and function of the outer membrane protein RCSF

Journal of Biological Chemistry

Volumn 286, Issue 21, 2011, Pages 18775-18783

  Rogov, Vladimir V ^a,b   Rogova, Natalia Yu ^a   Bernhard, Frank ^a   Löhr, Frank ^a   Dötsch, Volker ^a  

^a GOETHE UNIVERSITY   (Germany)

^b INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

AUXILIARY REGULATOR; BACTERIAL SIGNAL TRANSDUCTION; BIOFILM FORMATION; C-TERMINAL DOMAINS; CELL DIVISIONS; DISULFIDE BRIDGE; FULL-LENGTH PROTEINS; IN-VIVO; KEY ELEMENTS; MEMBRANE-BOUND; N-TERMINALS; OUTER MEMBRANE; OUTER MEMBRANE PROTEIN; POTENTIAL PARTNERS; SIGNALING CASCADES; SOLUBLE PROTEINS; STRUCTURAL ELEMENTS; WEAK INTERACTIONS;

BIOLOGICAL MEMBRANES; BIOSYNTHESIS; CELL PROLIFERATION; CHEMICAL ACTIVATION; COVALENT BONDS; GENES; GLUCOSE; RNA; SIGNAL TRANSDUCTION; SIGNALING;

PROTEINS;

ALANINE; CYSTEINE; GLYCINE; OUTER MEMBRANE PROTEIN; PROTEIN RCSF; RNA; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; BIOSYNTHESIS; CONTROLLED STUDY; CYTOPLASM; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN RNA BINDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS;

BACTERIAL OUTER MEMBRANE PROTEINS; BIOFILMS; CRYSTALLOGRAPHY, X-RAY; DISULFIDES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MUTATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SIGNAL TRANSDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP;

BACTERIA (MICROORGANISMS);

EID: 79956292587     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.230185     Document Type: Article

References (44)

1. Majdalani, N., and Gottesman, S. (2005) Annu. Rev. Microbiol. 59, 379-405
2. Gottesman, S., Trisler, P., and Torres-Cabassa, A. (1985) J. Bacteriol. 162, 1111-1119
3. Andresen, L., Kõiv, V., Alamäe, T., and Mäe, A. (2007) FEMS Microbiol. Lett. 273, 229-238
4. Francez-Charlot, A., Laugel, B., Van Gemert, A., Dubarry, N., Wiorowski, F., Castanié-Cornet, M. P., Gutierrez, C., and Cam, K. (2003) Mol. Microbiol. 49, 823-832
5. West, A. H., and Stock, A. M. (2001) Trends Biochem. Sci. 26, 369-376
6. Takeda, S., Fujisawa, Y., Matsubara, M., Aiba, H., and Mizuno, T. (2001) Mol. Microbiol. 40, 440-450
7. Chen, M. H., Takeda, S., Yamada, H., Ishii, Y., Yamashino, T., and Mizuno, T. (2001) Biosci. Biotechnol. Biochem. 65, 2364-2367
8. Gottesman, S., and Stout, V. (1991) Mol. Microbiol. 5, 1599-1606
9. Clarke, D. J., Joyce, S. A., Toutain, C. M., Jacq, A., and Holland, I. B. (2002) J. Bacteriol. 184, 1204-1208
10. Wehland, M., Kiecker, C., Coplin, D. L., Kelm, O., Saenger, W., and Bernhard, F. (1999) J. Biol. Chem. 274, 3300-3307
11. Wehland, M., and Bernhard, F. (2000) J. Biol. Chem. 275, 7013-7020
12. Pristovsek, P., Sengupta, K., Löhr, F., Schäfer, B., von Trebra, M. W., Rüterjans, H., and Bernhard, F. (2003) J. Biol. Chem. 278, 17752-17759
13. Rogov, V. V., Bernhard, F., Löhr, F., and Dötsch, V. (2004) J. Mol. Biol. 343, 1035-1048
14. Rogov, V. V., Rogova, N. Y., Bernhard, F., Koglin, A., Löhr, F., and Dötsch, V. (2006) J. Mol. Biol. 364, 68-79
15. Schmöe, K., Rogov, V. V., Rogova, N. Yu, Löhr, F., Güntert, P., Bernhard, F., and Dötsch, V. (2011) Structure 19, 577-587
16. Zhang, W., and Shi, L. (2005) Microbiology 151, 2159-2173
17. Majdalani, N., Heck, M., Stout, V., and Gottesman, S. (2005) J. Bacteriol. 187, 6770-6778
18. Castanie-Cornet, M. P., Cam, K., and Jacq, A. (2006) J. Bacteriol. 188, 4264-4270
19. Kadokura, H., Tian, H., Zander, T., Bardwell, J. C., and Beckwith, J. (2004) Science 303, 534-537
20. Farris, C., Sanowar, S., Bader, M. W., Pfuetzner, R., and Miller, S. I. (2010) J. Bacteriol. 192, 4894-4903
21. Callewaert, L., Vanoirbeek, K. G., Lurquin, I., Michiels, C. W., and Aertsen, A. (2009) J. Bacteriol. 191, 1979-1981
22. Laubacher, M. E., and Ades, S. E. (2008) J. Bacteriol. 190, 2065-2074
23. Sambrock, J., Fritsch, E. F., and Maniatis, T. (1989) in Molecular Cloning: A Laboratory Manual (Ford, N., Nolan, C., and Ferguson, M., eds) 2nd Ed., Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
24. Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. (1995) J. Biomol. NMR 6, 135-140
25. Rogov, V. V., Löhr, F., Rogova, N. Y., Klammt, C., Koglin, A., Bernhard, F., and Dötsch, V. (2007) J. Biomol. NMR 38, 165
26. Serber, Z., Selenko, P., Hänsel, R., Reckel, S., Löhr, F., Ferrell, J. E., Jr., Wagner, G., and Dötsch, V. (2006) Nat. Protoc. 1, 2701-2709
27. Serber, Z., Corsini, L., Durst, F., and Dötsch, V. (2005) Methods Enzymol. 394, 17-41
28. Goddard, T. D., and Kneller, D. G., SPARKY 3, University of California, San Francisco
29. Herrmann, T., Güntert, P., and Wüthrich, K. (2002) J. Mol. Biol. 319, 209-227
30. Güntert, P., Mumenthaler, C., and Wüthrich, K. (1997) J. Mol. Biol. 273, 283-298
31. Cornilescu, G., Delaglio, F., and Bax, A. (1999) J. Biomol. NMR 13, 289-302
32. Linge, J. P., Williams, M. A., Spronk, C. A., Bonvin, A. M., and Nilges, M. (2003) Proteins 50, 496-506
33. 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., Read, R. J., Rice, R. M., Simonson, T., and Warren, G. L. (1998) Acta Crystallogr. D Biol. Crystallogr. 54, 905-921
34. Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) J. Biomol. NMR 8, 477-486
35. Koradi, R., Billeter, M., and Wüthrich, K. (1996) J. Mol. Graph.14, 51-55
36. Bryson, K., McGuffin, L. J., Marsden, R. L., Ward, J. J., Sodhi, J. S., and Jones, D. T. (2005) Nucleic Acids Res. 33, W36-38
37. Seydel, A., Gounon, P., and Pugsley, A. P. (1999) Mol. Microbiol. 34, 810-821
38. Holm, L., and Sander, C. (1996) Science 273, 595-603
39. Hagiwara, D., Sugiura, M., Oshima, T., Mori, H., Aiba, H., Yamashino, T., and Mizuno, T. (2003) J. Bacteriol. 185, 5735-5746
40. Dubois, M., Gilles, K. A., Hamilton, J. K., Rebers, P. A., and Smith, F. (1956) Anal. Chem. 28, 350-356
41. Bernhard, F., Poetter, K., Geider, K., and Coplin, D. L. (1990) Mol. Plant-Microbe Interact. 3, 429-437
42. Clarke, D. J. (2010) Future Microbiol. 5, 1173-1184
43. Singh, P., Shaffer, S. A., Scherl, A., Holman, C., Pfuetzner, R. A., Larson Freeman, T. J., Miller, S. I., Hernandez, P., Appel, R. D., and Goodlett, D. R. (2008) Anal. Chem. 80, 8799-8806
44. Gervais, F. G., Phoenix, P., and Drapeau, G. R. (1992) J. Bacteriol. 174, 3964-3971