Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly

We report crystal structures of the Thermus thermophilus ribosome at 2.3- to 2.5-angstrom resolution, which have enabled modeling of rRNA modifications. The structures reveal contacts of modified nucleotides with mRNA and tRNAs or protein pY, and contacts within the ribosome interior stabilizing the functional fold of rRNA. Our work provides a resource to explore the roles of rRNA modifications and yields a more comprehensive atomic model of a bacterial ribosome.