Previous Article | Next Article 
J Bacteriol. 1987 January; 169(1): 283-290
Escherichia coli dnaK null mutants are inviable at high temperature.
K H Paek and
G C Walker
ABSTRACT
DnaK, a major Escherichia coli heat shock protein, is homologous to major heat shock proteins (Hsp70s) of Drosophila melanogaster and humans. Null mutations of the dnaK gene, both insertions and a deletion, were constructed in vitro and substituted for dnaK+ in the E. coli genome by homologous recombination in a recB recC sbcB strain. Cells carrying these dnaK null mutations grew slowly at low temperatures (30 and 37 degrees C) and could not form colonies at a high temperature (42 degrees C); furthermore, they also formed long filaments at 42 degrees C. The shift of the mutants to a high temperature evidently resulted in a loss of cell viability rather than simply an inhibition of growth since cells that had been incubated at 42 degrees C for 2 h were no longer capable of forming colonies at 30 degrees C. The introduction of a plasmid carrying the dnaK+ gene into these mutants restored normal cell growth and cell division at 42 degrees C. These null mutants showed a high basal level of synthesis of heat shock proteins except for DnaK, which was completely absent. In addition, the synthesis of heat shock proteins after induction in these dnaK null mutants was prolonged compared with that in a dnaK+ strain. The well-characterized dnaK756 mutation causes similar phenotypes, suggesting that they are caused by a loss rather than an alteration of DnaK function. The filamentation observed when dnaK mutations were incubated at a high temperature was not suppressed by sulA or sulB mutations, which suppress SOS-induced filamentation.(ABSTRACT TRUNCATED AT 250 WORDS)
J Bacteriol. 1987 January; 169(1): 283-290
This article has been cited by other articles:
-
Rupprecht, E., Gathmann, S., Fuhrmann, E., Schneider, D.
(2007). Three different DnaK proteins are functionally expressed in the cyanobacterium Synechocystis sp. PCC 6803. Microbiology
153: 1828-1841
[Abstract]
[Full Text]
-
Liebscher, M., Jahreis, G., Lucke, C., Grabley, S., Raina, S., Schiene-Fischer, C.
(2007). Fatty Acyl Benzamido Antibacterials Based on Inhibition of DnaK-catalyzed Protein Folding. J. Biol. Chem.
282: 4437-4446
[Abstract]
[Full Text]
-
Kourennaia, O. V., Tsujikawa, L., deHaseth, P. L.
(2005). Mutational Analysis of Escherichia coli Heat Shock Transcription Factor Sigma 32 Reveals Similarities with Sigma 70 in Recognition of the -35 Promoter Element and Differences in Promoter DNA Melting and -10 Recognition. J. Bacteriol.
187: 6762-6769
[Abstract]
[Full Text]
-
Dubern, J.-F., Lagendijk, E. L., Lugtenberg, B. J. J., Bloemberg, G. V.
(2005). The Heat Shock Genes dnaK, dnaJ, and grpE Are Involved in Regulation of Putisolvin Biosynthesis in Pseudomonas putida PCL1445. J. Bacteriol.
187: 5967-5976
[Abstract]
[Full Text]
-
Chattopadhyay, M. K., Kern, R., Mistou, M.-Y., Dandekar, A. M., Uratsu, S. L., Richarme, G.
(2004). The Chemical Chaperone Proline Relieves the Thermosensitivity of a dnaK Deletion Mutant at 42{degrees}C. J. Bacteriol.
186: 8149-8152
[Abstract]
[Full Text]
-
Gur, E., Biran, D., Shechter, N., Genevaux, P., Georgopoulos, C., Ron, E. Z.
(2004). The Escherichia coli DjlA and CbpA Proteins Can Substitute for DnaJ in DnaK-Mediated Protein Disaggregation. J. Bacteriol.
186: 7236-7242
[Abstract]
[Full Text]
-
Lin, X., Momany, C., Momany, M.
(2003). SwoHp, a Nucleoside Diphosphate Kinase, Is Essential in Aspergillus nidulans. Eukaryot Cell
2: 1169-1177
[Abstract]
[Full Text]
-
Wang, Y., deHaseth, P. L.
(2003). Sigma 32-Dependent Promoter Activity In Vivo: Sequence Determinants of the groE Promoter. J. Bacteriol.
185: 5800-5806
[Abstract]
[Full Text]
-
Hoff, K. G., Cupp-Vickery, J. R., Vickery, L. E.
(2003). Contributions of the LPPVK Motif of the Iron-Sulfur Template Protein IscU to Interactions with the Hsc66-Hsc20 Chaperone System. J. Biol. Chem.
278: 37582-37589
[Abstract]
[Full Text]
-
Lopes Ferreira, N., Alix, J.-H.
(2002). The DnaK Chaperone Is Necessary for {alpha}-Complementation of {beta}-Galactosidase in Escherichia coli. J. Bacteriol.
184: 7047-7054
[Abstract]
[Full Text]
-
Hoff, K. G., Ta, D. T., Tapley, T. L., Silberg, J. J., Vickery, L. E.
(2002). Hsc66 Substrate Specificity Is Directed toward a Discrete Region of the Iron-Sulfur Cluster Template Protein IscU. J. Biol. Chem.
277: 27353-27359
[Abstract]
[Full Text]
-
Echave, P., Esparza-Ceron, M. A., Cabiscol, E., Tamarit, J., Ros, J., Membrillo-Hernandez, J., Lin, E. C. C.
(2002). DnaK dependence of mutant ethanol oxidoreductases evolved for aerobic function and protective role of the chaperone against protein oxidative damage in Escherichia coli. Proc. Natl. Acad. Sci. USA
99: 4626-4631
[Abstract]
[Full Text]
-
Narberhaus, F.
(2002). {alpha}-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone Network. Microbiol. Mol. Biol. Rev.
66: 64-93
[Abstract]
[Full Text]
-
Barthel, T. K., Zhang, J., Walker, G. C.
(2001). ATPase-Defective Derivatives of Escherichia coli DnaK That Behave Differently with Respect to ATP-Induced Conformational Change and Peptide Release. J. Bacteriol.
183: 5482-5490
[Abstract]
[Full Text]
-
Nimura, K., Takahashi, H., Yoshikawa, H.
(2001). Characterization of the dnaK Multigene Family in the Cyanobacterium Synechococcus sp. Strain PCC7942. J. Bacteriol.
183: 1320-1328
[Abstract]
[Full Text]
-
Homuth, G., Domm, S., Kleiner, D., Schumann, W.
(2000). Transcriptional Analysis of Major Heat Shock Genes of Helicobacter pylori. J. Bacteriol.
182: 4257-4263
[Abstract]
[Full Text]
-
Buchberger, A., Gassler, C. S., Buttner, M., McMacken, R., Bukau, B.
(1999). Functional Defects of the DnaK756 Mutant Chaperone of Escherichia coli Indicate Distinct Roles for Amino- and Carboxyl-terminal Residues in Substrate and Co-chaperone Interaction and Interdomain Communication. J. Biol. Chem.
274: 38017-38026
[Abstract]
[Full Text]
-
Barthel, T. K., Walker, G. C.
(1999). Inferences Concerning the ATPase Properties of DnaK and Other HSP70s Are Affected by the ADP Kinase Activity of Copurifying Nucleoside-diphosphate Kinase. J. Biol. Chem.
274: 36670-36678
[Abstract]
[Full Text]
-
Mogk, A., Bukau, B., Lutz, R., Schumann, W.
(1999). Construction and Analysis of Hybrid Escherichia coli-Bacillus subtilis dnaK Genes. J. Bacteriol.
181: 1971-1974
[Abstract]
[Full Text]
-
Chakrabarti, S., Sengupta, N., Chowdhury, R.
(1999). Role of DnaK in In Vitro and In Vivo Expression of Virulence Factors of Vibrio cholerae. Infect. Immun.
67: 1025-1033
[Abstract]
[Full Text]
-
Berlyn, M. K. B.
(1998). Linkage Map of Escherichia coli K-12, Edition 10: The Traditional Map. Microbiol. Mol. Biol. Rev.
62: 814-984
[Abstract]
[Full Text]
-
Koch, B., Kilstrup, M., Vogensen, F. K., Hammer, K.
(1998). Induced Levels of Heat Shock Proteins in a dnaK Mutant of Lactococcus lactis. J. Bacteriol.
180: 3873-3881
[Abstract]
[Full Text]
-
Zhang, Y., Ohashi, N., Rikihisa, Y.
(1998). Cloning of the Heat Shock Protein 70 (HSP70) Gene of Ehrlichia sennetsu and Differential Expression of HSP70 and HSP60 mRNA after Temperature Upshift. Infect. Immun.
66: 3106-3112
[Abstract]
[Full Text]
-
Rockabrand, D., Livers, K., Austin, T., Kaiser, R., Jensen, D., Burgess, R., Blum, P.
(1998). Roles of DnaK and RpoS in Starvation-Induced Thermotolerance of Escherichia coli. J. Bacteriol.
180: 846-854
[Abstract]
[Full Text]
-
Ogata, Y., Mizushima, T., Kataoka, K., Kita, K., Miki, T., Sekimizu, K.
(1996). DnaK Heat Shock Protein of Escherichia coli Maintains the Negative Supercoiling of DNA against Thermal Stress. J. Biol. Chem.
271: 29407-29414
[Abstract]
[Full Text]
-
Zhang, J., Walker, G. C.
(1996). Identification of Elements of the Peptide Binding Site of DnaK by Peptide Cross-linking. J. Biol. Chem.
271: 19668-19674
[Abstract]
[Full Text]
-
Kusukawa, N, Yura, T
(1988). Heat shock protein GroE of Escherichia coli: key protective roles against thermal stress.. Genes Dev.
2: 874-882
[Abstract]
-
Erickson, J W, Vaughn, V, Walter, W A, Neidhardt, F C, Gross, C A
(1987). Regulation of the promoters and transcripts of rpoH, the Escherichia coli heat shock regulatory gene.. Genes Dev.
1: 419-432
[Abstract]
-
Echave, P., Esparza-Ceron, M. A., Cabiscol, E., Tamarit, J., Ros, J., Membrillo-Hernandez, J., Lin, E. C. C.
(2002). DnaK dependence of mutant ethanol oxidoreductases evolved for aerobic function and protective role of the chaperone against protein oxidative damage in Escherichia coli. Proc. Natl. Acad. Sci. USA
99: 4626-4631
[Abstract]
[Full Text]
Copyright © 1987 by the American Society for Microbiology. All rights reserved.