Structural, biophysical, and biochemical studies indicate that the coupled translocation of mRNA and tRNA during protein synthesis is driven by the structural dynamics of ribosomal RNA.
Highlights the functional role of ribosomal RNA in enabling the structural dynamics required for mRNA and tRNA translocation during protein synthesis.
Ribosomes are remarkable ribonucleoprotein complexes that are responsible for protein synthesis in all forms of life. They polymerize polypeptide chains programmed by nucleotide sequences in messenger RNA in a mechanism mediated by transfer RNA. One of the most challenging problems in the ribosome field is to understand the mechanism of coupled translocation of mRNA and tRNA during the elongation phase of protein synthesis. In recent years, the results of structural, biophysical and biochemical studies have provided extensive evidence that translocation is based on the structural dynamics of the ribosome itself. Detailed structural analysis has shown that ribosome dynamics, like aminoacyl-tRNA selection and catalysis of peptide bond formation, is made possible by the properties of ribosomal RNA.
Noller et al. (Sun,) reported a review. Structural, biophysical, and biochemical studies indicate that the coupled translocation of mRNA and tRNA during protein synthesis is driven by the structural dynamics of ribosomal RNA.