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A recombinant yeast bio-chassis for the isolation, characterization and cloning of human RNAseP.
We have used a recombinant yeast vector to express human and yeast RNAseP, the major constituent of the RNAseP/RPP30 ribonucleoprotein particle (RNP), and a recombinant yeast cell line to isolate the yeast enzyme. A (His)(6)-tagged RNAseP variant was expressed in high yield as a soluble, active enzyme in the yeast cytosol. The chimeric enzyme was purified by affinity chromatography using a (His)(6)-tag, and was examined in detail by negative-stain electron microscopy, size-exclusion chromatography, and electron paramagnetic resonance spectroscopy. The recombinant enzyme was effectively crystallized and its structure was determined at 2.3 A. The structure indicated that the (His)(6)-tag did not interfere with the secondary structure of the RNAseP monomer, but induced a change in quaternary structure, particularly in the N-terminal region. The isolated RNAseP was used for the construction of a yeast shuttle vector containing the human RNAseP cDNA. This vector was transformed into a haploid strain of Saccharomyces cerevisiae and three clones were selected. These clones integrated the cDNA into their genome and exhibited high levels of endogenous RNAseP activity, as detected by thin layer isoelectric focusing of whole cell extract. No higher than trace amounts of active recombinant RNAseP were detected in the clones. Three yeast RNAseP variants were isolated from two clones. This recombinant bio-chassis shows that the (His)(6)-tag does not alter the activity of RNAseP, whereas the yeast host provides the necessary facilities to perform a range of biotechnological

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