The catalytic RNA (H1 RNA) of the human nuclear tRNA processing enzyme RNase P has >105-fold lower activity than bacterial RNase P RNAs without its 11 protein cofactors. By introducing mutations toward the bacterial consensus into its catalytic domain, a 2- and 5-fold activity enhancement was achieved, laying the foundation for further ribozyme activity improvements via a combination of rational design and in vitro selection approaches. Will such reverse evolution reveal novel mechanistic solutions for tRNA processing by the ribozyme? More details can be found in the Research Article by Roland K. Hartmann and co-workers (DOI: 10.1002/cbic.202500803).
Li et al. (Thu,) studied this question.