JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lopes Ferreira, N.
Right arrow Articles by Alix, J.-H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lopes Ferreira, N.
Right arrow Articles by Alix, J.-H.

 Previous Article  |  Next Article 

Journal of Bacteriology, December 2002, p. 7047-7054, Vol. 184, No. 24
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.24.7047-7054.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

The DnaK Chaperone Is Necessary for {alpha}-Complementation of ß-Galactosidase in Escherichia coli

Nicolas Lopes Ferreira and Jean-Hervé Alix*

Institut de Biologie Physico-Chimique, U.P.R. 9073 du C.N.R.S. and Université Paris 7-Denis Diderot, F-75005 Paris, France

Received 24 July 2002/ Returned for modification 29 August 2002/ Accepted 19 September 2002

We show here the involvement of the molecular chaperone DnaK from Escherichia coli in the in vivo {alpha}-complementation of the ß-galactosidase. In the dnaK756(Ts) mutant, {alpha}-complementation occurs when the organisms are grown at 30°C but not at 37 or 40°C, although these temperatures are permissive for bacterial growth. Plasmid-driven expression of wild-type dnaK restores the {alpha}-complementation in the mutant but also stimulates it in a dnaK+ strain. In a mutant which contains a disrupted dnaK gene ({Delta}dnaK52::Cmr), {alpha}-complementation is also impaired, even at 30°C. This observation provides an easy and original phenotype to detect subtle functional changes in a protein such as the DnaK756 chaperone, within the physiologically relevant temperature.

* Corresponding author. Mailing address: Institut de Biologie Physico-Chimique, U.P.R. 9073 du C.N.R.S., 13 rue Pierre et Marie Curie, F-75005 Paris, France. Phone: (33) (1) 58 41 51 35. Fax: (33) (1) 58 41 50 20. E-mail: alix{at}ibpc.fr.

Journal of Bacteriology, December 2002, p. 7047-7054, Vol. 184, No. 24
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.24.7047-7054.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 2002 by the American Society for Microbiology. All rights reserved.