Molecular analysis of the multiple groEL proteins of chlamydiae

Journal of Bacteriology

Volumn 185, Issue 6, 2003, Pages 1958-1966

  Karunakaran, Karuna P ^a   Noguchi, Yasuyuki ^a   Read, Timothy D ^d   Cherkasov, Artem ^b   Kwee, Jeffrey ^a   Shen, Caixia ^a   Nelson, Colleen C ^c   Brunham, Robert C ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^b BRITISH COLUMBIA CANCER AGENCY   (Canada)

^c VANCOUVER GENERAL HOSPITAL   (Canada)

^d J CRAIG VENTER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN; CHAPERONIN 1; CHAPERONIN 2; CHAPERONIN 3; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENOME; BACTERIUM MUTANT; CHLAMYDIA; CHLAMYDIA TRACHOMATIS; CHLAMYDOPHILA PNEUMONIAE; CONTROLLED STUDY; DNA MICROARRAY; DNA TEMPLATE; ESCHERICHIA COLI; GENE; GENE EXPRESSION; GENE GROEL1; GENE GROEL2; GENE GROEL3; GENE STRUCTURE; HEAT SHOCK; HUMAN; HUMAN CELL; MOLECULAR GENETICS; MOLECULAR MODEL; NONHUMAN; NUCLEOTIDE SEQUENCE; PATHOGENESIS; PHYLOGENY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STRUCTURE; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STOICHIOMETRY; TRANSCRIPTION REGULATION; WESTERN BLOTTING;

AMINO ACID SEQUENCE; CHLAMYDIA TRACHOMATIS; ESCHERICHIA COLI; GENETIC COMPLEMENTATION TEST; GROEL PROTEIN; HEAT; HELA CELLS; HUMANS; MOLECULAR SEQUENCE DATA; PHYLOGENY; RECOMBINANT PROTEINS; SEQUENCE ANALYSIS, DNA;

BACTERIA (MICROORGANISMS); CHLAMYDIA TRACHOMATIS; CHLAMYDIAE; CHLAMYDOPHILA PNEUMONIAE; ESCHERICHIA COLI; NEGIBACTERIA; PROKARYOTA;

EID: 0037336256     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.6.1958-1966.2003     Document Type: Article

References (41)

1. Altschul, S. F., W. Gish, W. Miller, E. W. Myers, and D. J. Lipman. 1990. Basic local alignment search tool. J. Mol. Biol. 215:403-410.
2. Boisvert, D. C., J. Wang, Z. Otwinowski, A. L. Horwich, and P. B. Sigler. 1996. The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S. Nat. Struct. Biol. 3:170-177.
3. Branden, C., and J. Tooze. 1991. Introduction to protein structure. Garland Publishers, Inc., New York, N.Y.
4. Brunham, R. C., and R. W. Peeling. 1994. Chlamydia trachomatis antigens: role in immunity and pathogenesis. Infect. Agents Dis. 3:218-233.
5. Bryant, S. H., and S. F. Altschul. 1995. Statistics of sequence-structure threading. Curr. Opin. Struct. Biol. 5:236-244.
6. Capela, D., F. Barloy-Hubler, J. Gouzy, G. Bothe, F. Ampe, J. Batut, P. Boistard, A. Becker, M. Boutry, E. Cadieu, S. Dreano, S. Gloux, T. Godrie, A. Goffeau, D. Kahn, E. Kiss, V. Lelaure, D. Masuy, T. Pohl, D. Portetelle, A. Puhler, B. Purnelle, U. Ramsperger, C. Renard, P. Thebault, M. Vandenbol, S. Weidner, and F. Galibert. 2001. Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021. Proc. Natl. Acad. Sci. USA 98:9877-9882.
7. de Leon, P., S. Marco, C. Isiegas, A. Marina, J. L. Carrascosa, and R. P. Mellado. 1997. Streptomyces lividans groES, groEL1, and groEL2 genes. Microbiology 143:3563-3571.
8. Engel, J. N., J. Pollack, E. Perara, and D. Ganem. 1990. Heat shock response of murine Chlamydia trachomatis. J. Bacteriol. 172:6959-6972.
9. Everett, K. D., R. M. Bush, and A. A. Andersen. 1999. Emended description of the order Chlamydiales, proposal of Parachlamydiaceae fam. nov. and Simkaniaceae fam. nov., each containing one monotypic genus, revised taxonomy of the family Chlamydiaceae, including a new genus and five new species, and standards for the identification of organisms. Int. J. Syst. Bacteriol. 49(Pt. 2):415-440.
10. Fares, M. A., M. X. Ruiz-Gonzalez, A. Moya, S. F. Elena, and E. Barrio. 2002. Endosymbiotic bacteria: groEL buffers against deleterious mutations. Nature 417:398.
11. Fayet, O., T. Ziegelhoffer, and C. Georgopoulos. 1989. The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J. Bacteriol. 171:1379-1385.
12. Fenton, W. A., Y. Kashi, K. Furtak, and A. L. Horwich. 1994. Residues in chaperonin GroEL required for polypeptide binding and release. Nature 371:614-619.
13. Fischer, H. M., M. Babst, T. Kaspar, G. Acuna, F. Arigoni, and H. Hennecke. 1993. One member of a groESL-like chaperonin multigene family in Bradyrhizobium japonicum is co-regulated with symbiotic nitrogen fixation genes. EMBO J. 12:2901-2912.
14. Godzik, A., and J. Skolnick. 1992. Sequence-structure matching in globular proteins: application to supersecondary and tertiary structure determination. Proc. Natl. Acad. Sci. USA 89:12098-12102.
15. Gupta, R. S. 1996. Evolutionary relationships of chaperonins, p. 65-90. In R. J. Ellis (ed.), The chaperonins. Academic Press, Inc., San Diego, Calif.
16. Guzman, L. M., D. Belin, M. J. Carson, and J. Beckwith. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4230.
17. Jones, D. T., R. T. Miller, and J. M. Thornton. 1995. Successful protein fold recognition by optimal sequence threading validated by rigorous blind testing. Proteins 23:387-397.
18. Jones, D. T., W. R. Taylor, and J. M. Thornton. 1992. A new approach to protein fold recognition. Nature 358:86-89.
19. Karlin, S., L. Brocchieri, J. Mrazek, A. M. Campbell, and A. M. Spormann. 1999. A chimeric prokaryotic ancestry of mitochondria and primitive eukaryotes. Proc. Natl. Acad. Sci. USA 96:9190-9195.
20. Karlin, S., and J. Mrazek. 2000. Predicted highly expressed genes of diverse prokaryotic genomes. J. Bacteriol. 182:5238-5250.
21. Kong, T. H., A. R. Coates, P. D. Butcher, C. J. Hickman, and T. M. Shinnick. 1993. Mycobacterium tuberculosis expresses two chaperonin-60 homologs. Proc. Natl. Acad. Sci. USA 90:2608-2612.
22. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
23. Maniatis, T., E. F. Fritsch, and J. Sambrook. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
24. Mayhew, M., A. C. da Silva, J. Martin, H. Erdjument-Bromage, P. Tempst, and F. U. Hartl. 1996. Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Nature 379:420-426.
25. McLennan, N. F., A. S. Girshovich, N. M. Lissin, Y. Charters, and M. Masters. 1993. The strongly conserved carboxyl-terminus glycine-methionine motif of the Escherichia coli GroEL chaperonin is dispensable. Mol. Microbiol. 7:49-58.
26. Mizunoe, Y., S. N. Wai, K. Umene, T. Kokubo, S. Kawabata, and S. Yoshida. 1999. Cloning, sequencing, and functional expression in Escherichia coli of chaperonin (groESL) genes from Vibrio cholerae. Microbiol. Immunol. 43: 513-520.
27. Moran, N. A. 1996. Accelerated evolution and Muller's rachet in endosym-biotic bacteria. Proc. Natl. Acad. Sci. USA 93:2873-2878.
28. Murzin, A. G., and A. Bateman. 1997. Distant homology recognition using structural classification of proteins. Proteins 1(Suppl.):105-112.
29. Orengo, C. A. 1994. Classification of protein folds. Curr. Opin. Struct. Biol. 4:429-440.
30. Pawlowski, K., L. Jaroszewski, L. Rychlewski, and A. Godzik. 2000. Sensitive sequence comparison as protein function predictor. Pac. Symp. Biocomput. 2000:42-53.
31. Rinke de Wit, T. F., S. Bekelie, A. Osland, T. L. Miko, P. W. Hermans, D. van Soolingen, J. W. Drijfhout, R. Schoningh, A. A. Janson, and J. E. Thole. 1992. Mycobacteria contain two groEL genes: the second Mycobacterium leprae groEL gene is arranged in an operon with groES. Mol. Microbiol. 6:1995-2007.
32. Rusanganwa, E., and R. S. Gupta. 1993. Cloning and characterization of multiple groEL chaperonin-encoding genes in Rhizobium meliloti. Gene 126: 67-75.
33. Sanchez, R., and A. Sali. 1997. Evaluation of comparative protein structure modeling by MODELLER-3. Proteins 1(Suppl.):50-58.
34. Tan, M., B. Wong, and J. N. Engel. 1996. Transcriptional organization and regulation of the dnaK and groE operons of Chlamydia trachomatis. J. Bacteriol. 178:6983-6990.
35. Tanaka, N., T. Hiyama, and H. Nakamoto. 1997. Cloning, characterization and functional analysis of groESL operon from thermophilic cyanobacterium Synechococcus vulcanus. Biochim. Biophys. Acta 1343:335-348.
36. Taylor, W. R. 1997. Multiple sequence threading: an analysis of alignment quality and stability. J. Mol. Biol. 269:902-943.
37. Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
38. Vabulas, R. M., P. Ahmad-Nejad, C. da Costa, T. Miethke, C. J. Kirschning, H. Hacker, and H. Wagner. 2001. Endocytosed HSP60s use Toll-like receptor 2 (TLR2) and TLR4 to activate the Toll/interleukin-1 receptor signaling pathway in innate immune cells. J. Biol. Chem. 276:31332-31339.
39. Weissman, J. S., H. S. Rye, W. A. Fenton, J. M. Beechem, and A. L. Horwich. 1996. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell 84:481-490.
40. Young, R. A., and T. J. Elliott. 1989. Stress proteins, infection, and immune surveillance. Cell 59:5-8.
41. Zugel, U., and S. H. Kaufmann. 1999. Role of heat shock proteins in protection from and pathogenesis of infectious diseases. Clin. Microbiol. Rev. 12:19-39.