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Journal of Bacteriology, March 1999, p. 1971-1974, Vol. 181, No. 6
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Construction and Analysis of Hybrid Escherichia coli-Bacillus subtilis dnaK Genes

Axel Mogk,1,2 Bernd Bukau,2 Rolf Lutz,3 and Wolfgang Schumann1,*

Institute of Genetics, University of Bayreuth, D-95440 Bayreuth,1 Institute of Biochemistry and Molecular Biology, University of Freiburg, 79104 Freiburg,2 and Boehringer Mannheim GmbH, 82377 Penzberg,3 Germany

Received 24 September 1998/Accepted 11 January 1999

The highly conserved DnaK chaperones consist of an N-terminal ATPase domain, a central substrate-binding domain, and a C-terminal domain whose function is not known. Since Bacillus subtilis dnaK was not able to complement an Escherichia coli dnaK null mutant, we performed domain element swap experiments to identify the regions responsible for this finding. It turned out that the B. subtilis DnaK protein needed approximately normal amounts of the cochaperone DnaJ to be functional in E. coli. The ATPase domain and the substrate-binding domain form a species-specific functional unit, while the C-terminal domains, although less conserved, are exchangeable. Deletion of the C-terminal domain in E. coli DnaK affected neither complementation of growth at high temperatures nor propagation of phage lambda  but abolished degradation of sigma 32.

* Corresponding author. Mailing address: Institute of Genetics, University of Bayreuth, D-95440 Bayreuth, Germany. Phone: 0049 921 552708. Fax: 0049 921 552710. E-mail: wolfgang.schumann{at}uni-bayreuth.de.

Journal of Bacteriology, March 1999, p. 1971-1974, Vol. 181, No. 6
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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