Filamentous morphology in GroE-depleted Escherichia coli induced by impaired folding of FtsE

Journal of Bacteriology

Volumn 189, Issue 16, 2007, Pages 5860-5866

  Fujiwara, Kei ^a   Taguchi, Hideki ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CELL PROTEIN; CHAPERONIN; FTSZ PROTEIN; PROTEIN FTSA; PROTEIN FTSE; PROTEIN FTSQ; PROTEIN ZIPA; PROTEOME; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL VIABILITY; CELL DIVISION; ESCHERICHIA COLI; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEOMICS; STRUCTURE ANALYSIS;

ATP-BINDING CASSETTE TRANSPORTERS; CHAPERONINS; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEAT-SHOCK PROTEINS; PROTEIN FOLDING;

ESCHERICHIA COLI;

EID: 34547743871     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00493-07     Document Type: Article

References (31)

1. Aarsman, M. E., A. Piette, C. Fraipont, T. M. Vinkenvleugel, M. Nguyen-Disteche, and T. den Blaauwen. 2005. Maturation of the Escherichia coli divisome occurs in two steps. Mol. Microbiol. 55:1631-1645.
2. Bukau, B., and A. L. Horwich. 1998. The Hsp70 and Hsp60 chaperone machines. Cell 92:351-366.
3. Chapman, E., G. W. Farr, R. Usaite, K. Furtak, W. A. Fenton, T. K. Chaudhuri, E. R. Hondorp, R. G. Matthews, S. G. Wolf, J. R. Yates, M. Pypaert, and A. L. Horwich. 2006. Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL. Proc. Natl. Acad. Sci. USA 103:15800-15805.
4. Dam, M., and K. Gerdes. 1994. Partitioning of plasmid R1. Ten direct repeats flanking the parA promoter constitute a centromere-like partition site parC, that expresses incompatibility. J. Mol. Biol. 236:1289-1298.
5. de Leeuw, E., B. Graham, G. J. Phillips, C. M. ten Hagen-Jongman, B. Oudega, and J. Luirink. 1999. Molecular characterization of Escherichia coli FtsE and FtsX. Mol. Microbiol. 31:983-993.
6. Ewalt, K. L., J. P. Hendrick, W. A. Houry, and F. U. Hartl. 1997. In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell 90:491-500.
7. Fayet, O., T. Ziegelhoffer, and C. Georgopoulos. 1989. The groES and groEL heat shock genes of Escherichia coli are essential for bacterial growth at all temperatures. J. Bacteriol. 171:1379-1385.
8. Georgopoulos, C. P., and H. Eisen. 1974. Bacterial mutants which block phage assembly. J. Supramol. Struct. 2:349-359.
9. Gerdes, S. Y., M. D. Scholle, J. W. Campbell, G. Balazsi, E. Ravasz, M. D. Daugherty, A. L. Somera, N. C. Kyrpides, I. Anderson, M. S. Gelfand, A. Bhattacharya, V. Kapatral, M. D'Souza, M. V. Baev, Y. Grechkin, F. Mseeh, M. Y. Fonstein, R. Overbeek, A. L. Barabasi, Z. N. Oltvai, and A. L. Osterman. 2003. Experimental determination and system level analysis of essential genes in Escherichia coli MG1655. J. Bacteriol. 185:5673-5684.
10. Goehring, N. W., M. D. Gonzalez, and J. Beckwith. 2006. Premature targeting of cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly. Mol. Microbiol. 61:33-45.
11. Goloubinoff, P., J. T. Christeller, A. A. Gatenby, and G. H. Lorimer. 1989. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP. Nature 342:884-889.
12. Hartl, F. U., and M. Hayer-Hartl. 2002. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295:1852-1858.
13. Horwich, A. L., K. B. Low, W. A. Fenton, I. N. Hirshfield, and K. Furtak. 1993. Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell 74:909-917.
14. Houry, W. A., D. Frishman, C. Eckerskorn, F. Lottspeich, and F. U. Hartl. 1999. Identification of in vivo substrates of the chaperonin GroEL. Nature 402:147-154.
15. Kanemori, M., H. Mori, and T. Yura. 1994. Effects of reduced levels of GroE chaperones on protein metabolism: growth of Escherichia coli. J. Bacteriol. 176:4235-4242.
16. Kato, J., Y. Nishimura, M. Yamada, H. Suzuki, and Y. Hirota. 1988. Gene organization in the region containing a new gene involved in chromosome partition in Escherichia coli. J. Bacteriol. 170:3967-3977.
17. Kawai-Noma, S., S. Ayano, C. G. Pack, M. Kinjo, M. Yoshida, K. Yasuda, and H. Taguchi. 2006. Dynamics of yeast prion aggregates in single living cells. Genes Cells 11:1085-1096.
18. Kerner, M. J., D. J. Naylor, Y. Ishihama, T. Maier, H. C. Chang, A. P. Stines, C. Georgopoulos, D. Frishman, M. Hayer-Hartl, M. Mann, and F. U. Hartl. 2005. Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell 122:209-220.
19. Lemos, J. A., Y. Luzardo, and R. A. Burne. 2007. Physiologic effects of forced down-regulation of dnaK and groEL expression in Streptococcus mutans. J. Bacteriol. 189:1582-1588.
20. McLennan, N., and M. Masters. 1998. GroE is vital for cell-wall synthesis. Nature 392:139.
21. Ogino, H., M. Wachi, A. Ishii, N. Iwai, T. Nishida, S. Yamada, K. Nagai, and M. Sugai. 2004. FtsZ-dependent localization of GroEL protein at possible division sites. Genes Cells 9:765-771.
22. Reddy, M. 2007. Role of FtsEX in cell division of Escherichia coli: viability of ftsEX mutants is dependent on functional SufI or high osmotic strength. J. Bacteriol. 189:98-108.
23. Sakikawa, C., H. Taguchi, Y. Makino, and M. Yoshida. 1999. On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES. J. Biol. Chem. 274:21251-21256.
24. Schmidt, K. L., N. D. Peterson, R. J. Kustusch, M. C. Wissel, B. Graham, G. J. Phillips, and D. S. Weiss. 2004. A predicted ABC transporter, FtsEX, is needed for cell division in Escherichia coli. J. Bacteriol. 186:785-793.
25. Shimamura, T., A. Koike-Takeshita, K. Yokoyama, R. Masui, N. Murai, M. Yoshida, H. Taguchi, and S. Iwata. 2004. Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity. Structure 12:1471-1480.
26. Shimizu, Y., A. Inoue, Y. Tomari, T. Suzuki, T. Yokogawa, K. Nishikawa, and T. Ueda. 2001. Cell-free translation reconstituted with purified components. Nat. Biotechnol. 19:751-755.
27. Susin, M. F., R. L. Baldini, F. Gueiros-Filho, and S. L. Gomes. 2006. GroES/GroEL and DnaK/DnaJ have distinct roles in stress responses and during cell cycle progression in Caulobacter crescentus. J. Bacteriol. 188:8044-8053.
28. Taschner, P. E., P. G. Huls, E. Pas, and C. L. Woldringh. 1988. Division behavior and shape changes in isogenic ftsZ, ftsQ, ftsA, pbpB, and ftsE cell division mutants of Escherichia coli during temperature shift experiments. J. Bacteriol. 170:1533-1540.
29. Weiss, D. S. 2004. Bacterial cell division and the septal ring. Mol. Microbiol. 54:588-597.
30. Ying, B. W., H. Taguchi, M. Kondo, and T. Ueda. 2005. Co-translational involvement of the chaperonin GroEL in the folding of newly translated polypeptides. J. Biol. Chem. 280:12035-12040.
31. Ying, B. W., H. Taguchi, H. Ueda, and T. Ueda. 2004. Chaperone-assisted folding of a single-chain antibody in a reconstituted translation system. Biochem. Biophys. Res. Commun. 320:1359-1364.