Tightly-orchestrated rearrangements govern catalytic center assembly of the ribosome

Yi Zhou, Sharmishtha Musalgaonkar, Arlen W. Johnson () and David W. Taylor ()
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Yi Zhou: University of Texas at Austin
Sharmishtha Musalgaonkar: University of Texas at Austin
Arlen W. Johnson: University of Texas at Austin
David W. Taylor: University of Texas at Austin

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: Abstract The catalytic activity of the ribosome is mediated by RNA, yet proteins are essential for the function of the peptidyl transferase center (PTC). In eukaryotes, final assembly of the PTC occurs in the cytoplasm by insertion of the ribosomal protein Rpl10 (uL16). We determine structures of six intermediates in late nuclear and cytoplasmic maturation of the large subunit that reveal a tightly-choreographed sequence of protein and RNA rearrangements controlling the insertion of Rpl10. We also determine the structure of the biogenesis factor Yvh1 and show how it promotes assembly of the P stalk, a critical element for recruitment of GTPases that drive translation. Together, our structures provide a blueprint for final assembly of a functional ribosome.

Date: 2019
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DOI: 10.1038/s41467-019-08880-0

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