Complementary role of two fragments of domain V of 23 S ribosomal RNA in protein folding

We have shown that the domain V of bacterial 23 S rRNA could fold denatured proteins to their active state. This segment of 23 S rRNA could further be split into two parts. One part containing mainly the central loop of domai n V could bind denatured human carbonic anhydrase I stably. This associatio n could be reversed by adding the other part of domain V. The released enzy me was directed in such a way by the central loop of domain V that it could now fold by itself to active form. This agrees with our earlier observatio n that proteins fold within the cell posttranslationally, a process that is completed after release of the newly synthesized polypeptide from the ribo some.