Genetic analysis of the structure and function of RNase P fromE. coli

Abstract

A brief review of the genetic studies on ribonuclease P (RNase P) from Escherichia coli is presented. Temperature-sensitive mutants of E. coli defective in tRNA processing were isolated by screening cells which were unable to synthesize a suppressor tRNA at restrictive temperature. Structural analysis of accumulated tRNA precursors showed that the isolated mutants were defective in RNase P activity. Analyses of the mutants revealed that the enzyme is essential for the synthesis of all tRNA molecules in cells and that the enzyme consists of two subunits. Analyses of the isolated mutants revealed a possible domain structure of the RNA subunit of the enzyme.

High-order framework nucleic acid for targeted-delivery of antisense peptide nucleic acids to overcome drug resistance

“…Due to its large molecule weight and the lack of positive charges, asPNA exhibits limited permeability across plasma membranes. 7 Various types of carriers, including peptides, 8 polymers, 9 and inorganic nanomaterials, 10 have emerged as potential breakthroughs for enhancing cellular uptake of asPNA. However, most carriers suffer from low cargo capacity, limited uniformity, and poor biocompatibility, as well as the incapability to engineer precisely spatially addressable surfaces for the realization of multiple functionalities.…”