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Journal of Bacteriology, September 1999, p. 5871-5875, Vol. 181, No. 18
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

A Single-Ring Mitochondrial Chaperonin (Hsp60-Hsp10) Can Substitute for GroEL-GroES In Vivo

Kåre L. Nielsen,1,dagger Neil McLennan,2,Dagger Millicent Masters,2 and Nicholas J. Cowan1,*

Department of Biochemistry, New York University Medical Center, New York, New York 10016,1 and Institute of Cell and Molecular Biology, University of Edinburgh, Edinburgh EH9 3JR, Scotland2

Received 23 March 1999/Accepted 10 June 1999

Chaperonins participate in the facilitated folding of a variety of proteins in vivo. To see whether the same spectrum of target proteins can be productively folded by the double-ring prokaryotic chaperonin GroEL-GroES and its single-ring human mitochondrial homolog, Hsp60-Hsp10, we expressed the latter in an Escherichia coli strain engineered so that the groE operon is under strict regulatory control. We found that expression of Hsp60-Hsp10 restores viability to cells that no longer express GroEL-GroES, formally demonstrating that Hsp60-Hsp10 can carry out all essential in vivo functions of GroEL-GroES.

* Corresponding author. Mailing address: Department of Biochemistry, New York University Medical Center, New York, NY 10016. Phone: (212) 263-5809. Fax: (212) 263-8166. E-mail: CowanN01{at}mcrcr6.med.nyu.edu.

dagger Present address: Laboratory of Biotechnology, Aalborg Universitet, Aalborg, Denmark.

Dagger Present address: CJD Surveillance Unit, Department of Pathology, University of Edinburgh, Western General Hospital, Edinburgh, Scotland.

Journal of Bacteriology, September 1999, p. 5871-5875, Vol. 181, No. 18
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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