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Updated: May 19, 2026

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In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
Published on: July 25, 2019
A conserved deubiquitinating enzyme controls cell growth by regulating RNA polymerase I stability
Lauren A Richardson1, Benjamin J Reed, J Michael Charette
1Department of Pharmacology, University of Washington, Seattle, 98195, USA.
Cell Reports
|August 21, 2012
Summary
The yeast deubiquitinating enzyme Ubp10 regulates ribosome production by stabilizing RNA polymerase I. This deubiquitination process is conserved in humans, highlighting its importance in eukaryotic cell growth.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Ribosome biogenesis is crucial for eukaryotic cell function.
- Regulation of ribosome biogenesis factors remains poorly understood.
- The yeast deubiquitinating enzyme Ubp10's role was previously unknown.
Purpose of the Study:
- To investigate the function and regulation of Ubp10 in ribosome biogenesis.
- To identify Ubp10's interacting partners and molecular targets.
- To determine if Ubp10's role in ribosome biogenesis is conserved in eukaryotes.
Main Methods:
- Yeast genetics and cell biology techniques.
- Proteomic analysis to identify protein interactions.
- Functional assays for rRNA processing and ribosome production.
Main Results:
- Ubp10 localizes to the nucleolus and is essential for optimal pre-rRNA and rRNA levels.
- Ubp10 deubiquitinates and stabilizes the largest subunit of RNA polymerase I (RNAPI).
- Human USP36 complements yeast Ubp10 function, indicating conserved regulation of RNAPI.
Conclusions:
- Ubp10/USP36 is a key regulator of rRNA production via RNAPI stabilization.
- Deubiquitination of RNAPI is a conserved mechanism for ribosome biogenesis.
- This pathway is critical for maintaining ribosome levels and cell growth.
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