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Polyubiquitin architecture editing on collided ribosomes maintains persistent RQC activity.

Shota Tomomatsu1,2, Yoshitaka Matsuo3, Fumiaki Ohtake4

  • 1Division of RNA and Gene Regulation, Institute of Medical Science, The University of Tokyo, Minato-Ku, 108-8639, Japan.

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|September 16, 2025
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Two deubiquitinating enzymes (DUBs), Ubp2 and Ubp3, edit ubiquitin chains on yeast uS10, promoting ribosome-associated quality control (RQC) and ensuring persistent RQC activity.

Keywords:
DeubiquitinaseQuality ControlRibosomeUbiquitin CodeUbiquitination

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Ribosome-associated quality control (RQC) manages stalled ribosomes.
  • K63-linked polyubiquitination of ribosomal protein uS10 is vital for RQC-trigger (RQT) complex recruitment.
  • Mechanisms of polyubiquitin maintenance and recycling on colliding ribosomes are not fully understood.

Purpose of the Study:

  • To elucidate the roles of deubiquitinating enzymes (DUBs) in ubiquitin chain editing and recycling during RQC.
  • To investigate how Ubp2 and Ubp3 influence polyubiquitin architecture on uS10.
  • To understand the impact of specific ubiquitin linkages on RQT-mediated ribosome dissociation.

Main Methods:

  • Yeast genetics and biochemistry.
  • Analysis of polyubiquitin chain composition on uS10.
  • Investigation of DUB activity in vitro and in vivo.

Main Results:

  • Ubp2 removes K63-linked polyubiquitin chains from uS10 on free 40S subunits for recycling.
  • Ubp3 cleaves K48-linked and mixed-linkage polyubiquitin chains from uS10 on translating ribosomes.
  • K48-linked ubiquitin chains on uS10 inhibit RQT-mediated ribosome dissociation.

Conclusions:

  • Ubp2 and Ubp3 are key DUBs that edit and recycle polyubiquitin chains on uS10.
  • These DUB activities are essential for maintaining sustained RQC function.
  • The ubiquitin code on uS10 regulates RQC progression and ribosome quality control.