Existence of abnormal protein aggregates in healthy Escherichia coli cells

Journal of Bacteriology

Volumn 190, Issue 3, 2008, Pages 887-893

  Maisonneuve, Etienne ^a   Fraysse, Laetitia ^a   Moinier, Danielle ^b   Dukan, Sam ^a,b  

^a AIX MARSEILLE UNIVERSITÉ   (France)

^b CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; CHAPERONIN; ENDOPEPTIDASE CLP; ENDOPEPTIDASE CLPX; HEAT SHOCK PROTEIN 70; PROTEIN DNAK; SERINE PROTEINASE;

ARTICLE; BACTERIAL CELL; BACTERIUM CULTURE; DETOXIFICATION; ESCHERICHIA COLI; MASS SPECTROMETRY; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN FOLDING;

AEROBIOSIS; CYTOSOL; ENDOPEPTIDASE CLP; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HSP70 HEAT-SHOCK PROTEINS; MOLECULAR CHAPERONES; PROTEIN DENATURATION; PROTEIN FOLDING; REACTIVE OXYGEN SPECIES; RIBOSOMAL PROTEINS;

ESCHERICHIA COLI;

EID: 38649135397     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01603-07     Document Type: Article

References (18)

1. Arrasate, M., S. Mitra, E. S. Schweitzer, M. R. Segal, and S. Finkbeiner. 2004. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431:805-810.
2. Baars, L., A. J. Ytterberg, D. Drew, S. Wagner, C. Thilo, K. J. van Wijk, and J. W. de Gier. 2006. Defining the role of the Escherichia coli chaperone SecB using comparative proteomics. J. Biol. Chem. 281:10024- 10034.
3. Baba, T., T. Ara, M. Hasegawa, Y. Takai, Y. Okumura, M. Baba, K. A. Datsenko, M. Tomita, B. L. Wanner, and H. Mori. 2006. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol. Syst. Biol. 2:1-11.
4. Ben-Zvi, A. P., and P. Goloubinoff. 2001. Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones. J. Struct. Biol. 135:84-93.
5. 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.
6. Conrad, C. C., J. Choi, C. A. Malakowsky, J. M. Talent, R. Dai, P. Marshall, and R. W. Gracy. 2001. Identification of protein carbonyls after two-dimensional electrophoresis. Proteomics 1:829-834.
7. Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
8. Deuerling, E., H. Patzelt, S. Vorderwulbecke, T. Rauch, G. Kramer, E. Schaffitzel, A. Mogk, A. Schulze-Specking, H. Langen, and B. Bukau. 2003. Trigger factor and DnaK possess overlapping substrate pools and binding specificities. Mol. Microbiol. 47:1317-1328.
9. Dougan, D. A., A. Mogk, and B. Bukau. 2002. Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question. Cell. Mol. Life Sci. 59:1607-1616.
10. Flynn, J. M., S. B. Neher, Y. I. Kim, R. T. Sauer, and T. A. Baker. 2003. Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol. Cell 11:671-683.
11. 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.
12. Rosen, R., D. Biran, E. Gur, D. Becher, M. Hecker, and E. Z. Ron. 2002. Protein aggregation in Escherichia coli: role of proteases. FEMS Microbiol. Lett. 207:9-12.
13. Rujano, M. A., F. Bosveld, F. A. Salomons, F. Dijk, M. A. van Waarde, J. J. van der Want, R. A. de Vos, E. R. Brunt, O. C. Sibon, and H. H. Kampinga. 2006. Polarised asymmetric inheritance of accumulated protein damage in higher eukaryotes. PLoS Biol. 4:e417.
14. Shevchenko, A., M. Wilm, O. Vorm, and M. Mann. 1996. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68:850-858.
15. Tomoyasu, T., A. Mogk, H. Langen, P. Goloubinoff, and B. Bukau. 2001. Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol. Mol. Microbiol. 40:397-413.
16. Tran, P. B., and R. J. Miller. 1999. Aggregates in neurodegenerative disease: crowds and power? Trends Neurosci. 22:194-197.
17. Wickner, S., M. R. Maurizi, and S. Gottesman. 1999. Posttranslational quality control: folding, refolding, and degrading proteins. Science 286:1888-1893.
18. Winter, J., K. Linke, A. Jatzek, and U. Jakob. 2005. Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33. Mol. Cell 17:381-392.