Ubiquitination of stalled ribosome triggers ribosome-associated quality control

Yoshitaka Matsuo, Ken Ikeuchi, Yasushi Saeki, Shintaro Iwasaki, Christian Schmidt, Tsuyoshi Udagawa, Fumiya Sato, Hikaru Tsuchiya, Thomas Becker, Keiji Tanaka, Nicholas T. Ingolia, Roland Beckmann and Toshifumi Inada ()
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Yoshitaka Matsuo: Tohoku University
Ken Ikeuchi: Tohoku University
Yasushi Saeki: Tokyo Metropolitan Institute of Medical Science
Shintaro Iwasaki: University of California
Christian Schmidt: University of Munich
Tsuyoshi Udagawa: Tohoku University
Fumiya Sato: Tohoku University
Hikaru Tsuchiya: Tokyo Metropolitan Institute of Medical Science
Thomas Becker: University of Munich
Keiji Tanaka: Tokyo Metropolitan Institute of Medical Science
Nicholas T. Ingolia: University of California
Roland Beckmann: University of Munich
Toshifumi Inada: Tohoku University

Nature Communications, 2017, vol. 8, issue 1, 1-14

Abstract: Abstract Translation arrest by polybasic sequences induces ribosome stalling, and the arrest product is degraded by the ribosome-mediated quality control (RQC) system. Here we report that ubiquitination of the 40S ribosomal protein uS10 by the E3 ubiquitin ligase Hel2 (or RQT1) is required for RQC. We identify a RQC-trigger (RQT) subcomplex composed of the RNA helicase-family protein Slh1/Rqt2, the ubiquitin-binding protein Cue3/Rqt3, and yKR023W/Rqt4 that is required for RQC. The defects in RQC of the RQT mutants correlate with sensitivity to anisomycin, which stalls ribosome at the rotated form. Cryo-electron microscopy analysis reveals that Hel2-bound ribosome are dominantly the rotated form with hybrid tRNAs. Ribosome profiling reveals that ribosomes stalled at the rotated state with specific pairs of codons at P-A sites serve as RQC substrates. Rqt1 specifically ubiquitinates these arrested ribosomes to target them to the RQT complex, allowing subsequent RQC reactions including dissociation of the stalled ribosome into subunits.

Date: 2017
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DOI: 10.1038/s41467-017-00188-1

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