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Journal of Bacteriology, December 2004, p. 8149-8152, Vol. 186, No. 23
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.23.8149-8152.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The Chemical Chaperone Proline Relieves the Thermosensitivity of a dnaK Deletion Mutant at 42°C

Madhab K. Chattopadhyay,1,{dagger} Renée Kern,1 Michel-Yves Mistou,2 Abhaya M. Dandekar,3 Sandra L. Uratsu,3 and Gilbert Richarme1*

Molécules de Stress, Institut Jacques Monod, Université Paris 7, Paris,1 Unité de Biochimie et Structure des Protéines, INRA, Jouy en Josas, France,2 Department of Pomology, University of California-Davis, Davis, California3

Received 18 June 2004/ Accepted 19 July 2004

Since, like other osmolytes, proline can act as a protein stabilizer, we investigated the thermoprotectant properties of proline in vitro and in vivo. In vivo, elevated proline pools in Escherichia coli (obtained by altering the feedback inhibition by proline of {gamma}-glutamylkinase, the first enzyme of the proline biosynthesis pathway) restore the viability of a dnaK-deficient mutant at 42°C, suggesting that proline can act as a thermoprotectant for E. coli cells. Furthermore, analysis of aggregated proteins in the dnaK-deficient strain at 42°C by two-dimensional gel electrophoresis shows that high proline pools reduce the protein aggregation defect of the dnaK-deficient strain. In vitro, like other "chemical chaperones," and like the DnaK chaperone, proline protects citrate synthase against thermodenaturation and stimulates citrate synthase renaturation after urea denaturation. These results show that a protein aggregation defect can be compensated for by a single mutation in an amino acid biosynthetic pathway and that an ubiquitously producible chemical chaperone can compensate for a defect in one of the major chaperones involved in protein folding and aggregation.

* Corresponding author. Mailing address: Molécules de Stress, Institut Jacques Monod, Université Paris 7, 2 place Jussieu, 75251 Paris Cedex 05, France. Phone: 33-1 44 27 50 98. Fax: 33-1 44 27 35 80. E-mail: richarme{at}ccr.jussieu.fr.

{dagger} Present address: Centre for Cellular and Molecular Biology, Hyderabad 500007, India.

Journal of Bacteriology, December 2004, p. 8149-8152, Vol. 186, No. 23
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.23.8149-8152.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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