PerspectiveMolecular Biology

The Eukaryotic Ribosome

+ See all authors and affiliations

Science  11 Feb 2011:
Vol. 331, Issue 6018, pp. 681-682
DOI: 10.1126/science.1202093

You are currently viewing the summary.

View Full Text


The past decade has seen a remarkable advance in our understanding of ribosomes, the large protein-RNA machines in all cells that use genetic information to synthesize proteins in a process known as translation. Ribosomes from all species consist of two subunits: a small subunit that decodes messenger RNA (mRNA), and a large subunit that catalyzes peptide bond formation between the growing polypeptide chain and each new amino acid. In 2000, researchers determined the atomic structures of the small and large ribosome subunits from bacteria and archaea, respectively. This has resulted in a dramatic increase in our understanding of translation in prokaryotes (1). On page 730 of this issue, Rabl et al. take an important step toward doing the same for eukaryotic translation. They offer a crystal structure of the small ribosomal subunit, together with a translation initiation protein, from the eukaryotic protozoan Tetrahymena thermophila (2). This structure, together with a crystal structure of the eukaryotic ribosome from the yeast Saccharomyces cerevisiae at a resolution of 4.15 Å (3) and a cryoelectron microscopy (cryo-EM) structure of a translating plant ribosome from Triticum aestivum at 5.5 Å (4, 5), represents a breakthrough in studying translation in eukaryotes.