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. Author manuscript; available in PMC: 2013 Sep 3.
Published in final edited form as: Methods Mol Biol. 2011;714:423–444. doi: 10.1007/978-1-61779-005-8_26

Fig. 2.

Fig. 2

Insertion of the streptavidin binding aptamer into ribonucleoprotein complexes. (Yeast RNase P and RNase MRP) Aptamer insertions into the yeast RNase MRP and RNase P holoenzymes have been used to purify these ribonucleoprotein complexes. The yeast RNase P has been extensively tagged, initially with the full SELEX derived sequence (shown) and subsequently with the minimal streptavidin binding aptamer sequence. The yeast RNase P can be tagged in four different locations that are indicated (*). In each case, these positions are known to be phylogenetically variable and solvent exposed and the aptamer insertion does not alter the growth or pre-tRNA processing significantly. (Yeast telomerase) The yeast telomerase was tagged at two positions, the successful aptamer insertion is shown and the unsuccessful position is also indicated (#). The purified telomerase was subsequently shown to be active in a telomerase assay. (Bacterial ribosomes) The streptavidin aptamer was used to specifically isolate ribosomal subunits containing a known lethal mutation. Coexpression of the lethal mutation alongside the wildtype sequence was necessary to sustain bacterial growth.