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Journal of Bacteriology, September 2001, p. 5198-5202, Vol. 183, No. 17
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.17.5198-5202.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Regulation and Mechanism of Action of the Small Heat Shock Protein from the Hyperthermophilic Archaeon Pyrococcus furiosus†

Pongpan Laksanalamai, Dennis L. Maeder, and Frank T. Robb*

Center of Marine Biotechnology, University of Maryland Biotechnology Institute, Baltimore, Maryland 21202

Received 5 January 2001/Accepted 4 June 2001

The small heat shock protein (sHSP) from the hyperthermophile Pyrococcus furiosus was specifically induced at the level of transcription by heat shock at 105°C. The gene encoding this protein was cloned and overexpressed in Escherichia coli. The recombinant sHSP prevented the majority of E. coli proteins from aggregating in vitro for up to 40 min at 105°C. The sHSP also prevented bovine glutamate dehydrogenase from aggregating at 56°C. Survivability of E. coli overexpressing the sHSP was enhanced approximately sixfold during exposure to 50°C for 2 h compared with the control culture, which did not express the sHSP. Apparently, the sHSP confers a survival advantage on mesophilic bacteria by preventing protein aggregation at supraoptimal temperatures.

* Corresponding author. Mailing address: Center of Marine Biotechnology, University of Maryland Biotechnology Institute, 701 E. Pratt St., Baltimore, MD 21202. Phone: (410) 234-8870. Fax: (410) 234-8896. E-mail: robb{at}umbi.umd.edu.

dagger Contribution 524 from the Center of Marine Biotechnology.

Journal of Bacteriology, September 2001, p. 5198-5202, Vol. 183, No. 17
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.17.5198-5202.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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