Assembly and functionality of the ribosome with tethered subunits

Nikolay A. Aleksashin, Margus Leppik, Adam J. Hockenberry, Dorota Klepacki, Nora Vázquez-Laslop, Michael C. Jewett, Jaanus Remme () and Alexander S. Mankin ()
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Nikolay A. Aleksashin: University of Illinois at Chicago
Margus Leppik: University of Tartu
Adam J. Hockenberry: Northwestern University
Dorota Klepacki: University of Illinois at Chicago
Nora Vázquez-Laslop: University of Illinois at Chicago
Michael C. Jewett: Northwestern University
Jaanus Remme: University of Tartu
Alexander S. Mankin: University of Illinois at Chicago

Nature Communications, 2019, vol. 10, issue 1, 1-13

Abstract: Abstract Ribo-T is an engineered ribosome whose small and large subunits are tethered together by linking 16S rRNA and 23S rRNA in a single molecule. Although Ribo-T can support cell proliferation in the absence of wild type ribosomes, Ribo-T cells grow slower than those with wild type ribosomes. Here, we show that cell growth defect is likely explained primarily by slow Ribo-T assembly rather than its imperfect functionality. Ribo-T maturation is stalled at a late assembly stage. Several post-transcriptional rRNA modifications and some ribosomal proteins are underrepresented in the accumulated assembly intermediates and rRNA ends are incompletely trimmed. Ribosome profiling of Ribo-T cells shows no defects in translation elongation but reveals somewhat higher occupancy by Ribo-T of the start codons and to a lesser extent stop codons, suggesting that subunit tethering mildly affects the initiation and termination stages of translation. Understanding limitations of Ribo-T system offers ways for its future development.

Date: 2019
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DOI: 10.1038/s41467-019-08892-w

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