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Journal of Bacteriology, July 1999, p. 4237-4244, Vol. 181, No. 14
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The Unique Chaperone Operon of Thermotoga maritima: Cloning and Initial Characterization of a Functional Hsp70 and Small Heat Shock Protein

Edward T. Michelini and Gregory C. Flynn*

Institute of Molecular Biology and Department of Chemistry, University of Oregon, Eugene, Oregon 97403

Received 17 November 1998/Accepted 14 May 1999

The hyperthermophilic eubacterium Thermotoga maritima possesses an operon encoding an Hsp70 molecular chaperone protein and a protein with meaningful homology to the small heat shock protein family of chaperones. This represents the first demonstrated co-operon organization for these two important classes of molecular chaperones. We have cloned and initially characterized these proteins as functional chaperones in vitro: the Hsp70 is capable of ATP hydrolysis and substrate binding, and the small heat shock protein can suppress protein aggregation and stably bind a refolding-competent substrate. In addition, the primary sequence of the Hsp70 is used to infer the phylogenetic relationships of T. maritima, one of the deepest-branching eubacteria known.

* Corresponding author. Mailing address: Institute of Molecular Biology, University of Oregon, Eugene, OR 97403. Phone: (541) 346-1535. Fax: (541) 346-5891. E-mail: gflynn{at}morel.uoregon.edu.

Journal of Bacteriology, July 1999, p. 4237-4244, Vol. 181, No. 14
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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