The involvement of RNA in ribosome function

  title={The involvement of RNA in ribosome function},
  author={Peter B Moore and Thomas A. Steitz},
The ribosome is a particle made of RNA and protein that is found in abundance in all cells that are actively making protein. It catalyses the messenger RNA-directed synthesis of proteins. Recent structural work has demonstrated a profound involvement of the ribosome's RNA component in all aspects of its function, supporting the hypothesis that proteins were added to the ribosome late in its evolution. 

5 S rRNA: structure and interactions.

This paper summarizes recently published data on the structure and function of 5 S rRNA and its interactions in complexes with proteins, within and outside the ribosome.

The ribosome and the mechanism of protein synthesis

Cryo-electron microscopy is starting to contribute toward the understanding of the ribosome's function, by portraying its conformational changes and binding interactions with the cofactors and tRNA.

Evolution and assembly of the ribosome

The complex history presented for “core” protein S4 suggests the existence of a gene pool before the emergence of bacterial lineages and reflects the pervasive nature of HGT in subsequent bacterial evolution, and is proven to be stable throughout the micro-second molecular dynamics simulations.

Structural Insight Into Functional Aspects of Ribosomal RNA Targeting

  • A. Yonath
  • Biology, Chemistry
    Chembiochem : a European journal of chemical biology
  • 2003
Recent advances in studies aimed at the understanding of the molecular mechanisms that are triggered, accomplished, or assisted by rRNA interactions are highlighted.

The structural basis of large ribosomal subunit function.

The work reviewed proves beyond doubt that the ribosome is an RNA enzyme, as had long been surmised on the basis of less conclusive evidence.

Ribosome, High Resolution Structure and Function

The structures show unequivocally that mainly ribosomal RNA is present in the peptidyl transferase center as well as in the decoding center, indicating that it is in fact ribosome RNA that is responsible for all aspects of peptide synthesis.

5.5 Å Structure of the Eukaryotic Ribosome

Cryo-electron microscopy and single-particle reconstruction provide insights into the structure, function and evolution of the eukaryotic translational apparatus with near-complete atomic models of the 80S ribosome.

Antibiotics and the ribosome

The recent progress, problems and new directions of research of ribosome‐targeting antibiotics are discussed in this review.



Ribosomes and translation.

Biochemical and genetic approaches have identified specific functional interactions involving conserved nucleotides in 16S and 23S rRNA and promise to yield an unprecedented view of the mechanism of translation in the coming years.

Direct Visualization of A-, P-, and E-Site Transfer RNAs in the Escherichia coli Ribosome

The detailed arrangement of A- and P-site tRNAs inferred from this study allows localization of the sites for anticodon interaction and peptide bond formation on the ribosome.

Structure, Function, and Genetics of Ribosomes

The papers in this book cover the Ribosome conference held at the University of Texas Marine Science Institute. The topics covered include: Structure of ribosomes; Self-organization of ribosomal RNA;

The elongation phase of protein synthesis.

Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics

The functional implications of the high-resolution 30S crystal structure are described, and details of the interactions between the 30S subunit and its tRNA and mRNA ligands are inferred, which lead to a model for the role of the universally conserved 16S RNA residues A1492 and A1493 in the decoding process.

Crystal structure of an initiation factor bound to the 30S ribosomal subunit.

The crystal structure of a complex of IF1 and the 30S ribosomal subunit is reported, explaining how localized changes at the ribosome A site lead to global alterations in the conformation of the30S subunit.

Visualization of elongation factor Tu on the Escherichia coli ribosome

Electron cryomicroscopy and angular reconstitution are used to visualize directly the kirromycin-stalled ternary complex in the A site of the 70S ribosome of Escherichia coli and three-dimensional reconstruction at 18 Å resolution shows the ternaries spanning the inter-subunit space with the acceptor domain of the tRNA reaching into the decoding centre.

A base pair between tRNA and 23S rRNA in the peptidyl transferase centre of the ribosome

Findings establish a direct role for 23S rRNA in protein synthesis and a Watson–Crick G–C pair between G2252 in a conserved hairpin loop of tRNA and C74 at the acceptor end of t RNA in the ribosomal P site.

A ratchet-like inter-subunit reorganization of the ribosome during translocation

Three-dimensional cryo-electron microscopy maps of the Escherichia coli 70S ribosome in various functional states show that both EF-G binding and subsequent GTP hydrolysis lead to ratchet-like rotations of the small 30S sub unit relative to the large 50S subunit, indicating a two-step mechanism of translocation.