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Ribosome origami

Nature Structural & Molecular Biology volume 24, pages 879–881 (2017)Cite this article

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Assembly of the small ribosomal subunit from an RNA strand and 33 proteins is an intricate and dynamic process. Two cryo-EM studies now provide insight into a complicated complex of at least 51 trans-factors that act on the preribosomal small subunit to sequentially fold it into a 3D molecular machine.

Remarkable advances in our understanding of protein translation have been possible thanks to structural biology studies revealing molecular mechanisms of how ribosomes synthesize proteins through a series of highly regulated steps. The efficiency, speed and control of this process relies on the structural complexity of the ribosome, which in eukaryotes is composed of ∼79 proteins and four rRNAs. Exactly how these ribosomal components are folded and combined into self-ruling, multifunctional units remains a fundamental question. Barandun et al.1 and Cheng et al.2, together with the recent work of Sun et al.3, visualize the processome by cryo-EM and report how the small subunit of the eukaryotic ribosome comes to be.

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Figure 1: Dissecting the small ribosomal subunit processome.

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Authors and Affiliations

  1. the Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden

    Joanna Rorbach

  2. the Department of Biochemistry and Biophysics, Science for Life Laboratory, Stockholm University, Solna, Sweden

    Shintaro Aibara & Alexey Amunts

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  1. Joanna Rorbach
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  2. Shintaro Aibara
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  3. Alexey Amunts
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Correspondence to Alexey Amunts.

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Rorbach, J., Aibara, S. & Amunts, A. Ribosome origami. Nat Struct Mol Biol 24, 879–881 (2017). https://doi.org/10.1038/nsmb.3497

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