PerspectivePROTEIN SYNTHESIS

The delicate dance of translation and folding

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Science  24 Apr 2015:
Vol. 348, Issue 6233, pp. 399-400
DOI: 10.1126/science.aab2157

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Summary

The past decade has seen rapid growth in our knowledge of how proteins are synthesized in cells. This includes the basic step of how transfer RNAs (tRNAs) decode messenger RNAs (mRNAs) with high fidelity and speed, how the ribosome moves along mRNA from codon to codon during translation, and how synthesis of the corresponding polypeptide chain is initiated and terminated at specific points on the mRNA (1). Structures of the ribosomal particles—megadalton RNA-protein assemblies—have provided detailed molecular views of the active sites for mRNA decoding and peptide bond formation, and suggested pathways for movement of ligands, factors, and the ribosomal subunits themselves. Obscured in this rich cache of knowledge is the fate of the protein product. How does it fold during mRNA translation and how might protein folding affect translation itself? These questions are addressed by elegant biophysical and biochemical approaches reported by Goldman et al. (2) and Kim et al. (3) on pages 457 and 444, respectively, of this issue, adding to a growing appreciation of cotranslational protein folding (46).