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Journal of Bacteriology, December 2000, p. 7092-7096, Vol. 182, No. 24
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The Truncated Form of the Bacterial Heat Shock Protein ClpB/HSP100 Contributes to Development of Thermotolerance in the Cyanobacterium Synechococcus sp. Strain PCC 7942

Adrian K. Clarke* and Mats-Jerry Eriksson

Umeå Plant Sciences Centre, Department of Plant Physiology, University of Umeå, Umeå S-901 87, Sweden

Received 17 July 2000/Accepted 23 September 2000

ClpB is a highly conserved heat shock protein that is essential for thermotolerance in bacteria and eukaryotes. One distinctive feature of all bacterial clpB genes is the dual translation of a truncated 79-kDa form (ClpB-79) in addition to the full-length 93-kDa protein (ClpB-93). To investigate the currently unknown function of ClpB-79, we have examined the ability of the two different-sized ClpB homologues from the cyanobacterium Synechococcus sp. strain PCC 7942 to confer thermotolerance. We show that the ClpB-79 form has the same capacity as ClpB-93 to confer thermotolerance and that the ClpB-79 protein contributes ca. one-third of the total thermotolerance developed in wild-type Synechococcus, the first in vivo demonstration of a functional role for ClpB-79 in bacteria.

* Corresponding author. Mailing address: Umeå Plant Sciences Center, Department of Plant Physiology, University of Umeå, Umeå S-901 87, Sweden. Phone: 46 90 7865209. Fax: 46 90 7866676. E-mail: Adrian.Clarke{at}plantphys.umu.se.

Journal of Bacteriology, December 2000, p. 7092-7096, Vol. 182, No. 24
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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