Site-Specific K63 Ubiquitinomics Provides Insights into Translation Regulation under Stress

Songhee Back, Andrew W. Gorman, Christine Vogel, Gustavo M. Silva

Research output: Contribution to journalArticlepeer-review


During oxidative stress, K63-linked polyubiquitin chains modify a variety of proteins including ribosomes. Knowledge of the precise sites of K63 ubiquitin is key to understand its function during the response to stress. To identify the sites of K63 ubiquitin, we developed a new mass spectrometry based method that quantified >1100 K63 ubiquitination sites in yeast that responded to oxidative stress induced by H 2 O 2 . We determined that under stress, K63 ubiquitin-modified proteins were involved in several cellular functions including ion transport, protein trafficking, and translation. The most abundant ubiquitin sites localized to the head of the 40S subunit of the ribosome, modified assembled polysomes, and affected the binding of translation factors. The results suggested a new pathway of post-initiation control of translation during oxidative stress and illustrated the importance of high-resolution mapping of noncanonical ubiquitination events.

Original languageEnglish (US)
Pages (from-to)309-318
Number of pages10
JournalJournal of Proteome Research
Issue number1
StatePublished - Jan 4 2019


  • K63 ubiquitin
  • oxidative stress
  • proteomics
  • ribosome
  • translational control

ASJC Scopus subject areas

  • Biochemistry
  • General Chemistry


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