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The hyperthermophilic eubacteriumThermotoga 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 ofT. maritima , one of the deepest-branching eubacteria known.

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