Abstract
A high-resolution structure of the eukaryotic ribosome has been determined, leading to increased interest in studying protein biosynthesis and its regulation in the cell. New functional complexes of the full ribosome crystals obtained from the bacteria Escherichia coli and Thermus thermophilus and the yeast Saccharomyces cerevisiae have permitted the identification of precise residue positions in different states of the ribosome function. This knowledge, together with electron microscopy studies, has improved the understanding of how basic ribosome processes, including mRNA decoding, peptide bond formation, mRNA and tRNA translocation, and co-translational transport and modifications of the nascent peptide are regulated.
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