The sigma factor σ of the obligate intracytoplasmic bacterium was overexpressed and purified from The rickettsial gene encoding σ was cloned into a -cleaved pET15b vector under control of T7 transcription and translation signals. The recombinant plasmid encoded a 75 kDa fusion protein that was overproduced in BL21(DE3) and purified from inclusion bodies after solubilization with guanidine hydrochloride and using His. Bind metal chelation resin. The N-terminal His. Tag sequence of the 75 kDa fusion protein was removed by thrombin treatment to obtain σ. The σ as well as the 75 kDa fusion protein had the ability to bind to core DNA-dependent RNA polymerase of both and and to stimulate their interaction with a rickettsial promoter.


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