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

Journal Article (Journal Article)

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 H2 O2 . 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.

Full Text

Duke Authors

Cited Authors

  • Back, S; Gorman, AW; Vogel, C; Silva, GM

Published Date

  • January 2019

Published In

Volume / Issue

  • 18 / 1

Start / End Page

  • 309 - 318

PubMed ID

  • 30489083

Pubmed Central ID

  • PMC6465141

Electronic International Standard Serial Number (EISSN)

  • 1535-3907

International Standard Serial Number (ISSN)

  • 1535-3893

Digital Object Identifier (DOI)

  • 10.1021/acs.jproteome.8b00623


  • eng