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 journalArticle

Abstract

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 H2O2. 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)
JournalJournal of Proteome Research
DOIs
StateAccepted/In press - Jan 1 2018

Fingerprint

Ubiquitin
Oxidative stress
Oxidative Stress
Ubiquitination
Eukaryotic Small Ribosome Subunits
Polyubiquitin
Polyribosomes
Ion Transport
Protein Biosynthesis
Protein Transport
Ribosomes
Yeast
Mass spectrometry
Mass Spectrometry
Carrier Proteins
Proteins
Yeasts
Ions

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)

Cite this

Site-Specific K63 Ubiquitinomics Provides Insights into Translation Regulation under Stress. / Back, Songhee; Gorman, Andrew W.; Vogel, Christine; Silva, Gustavo M.

In: Journal of Proteome Research, 01.01.2018.

Research output: Contribution to journalArticle

@article{95896d6c66b041558b6be2bd0c7d7c84,
title = "Site-Specific K63 Ubiquitinomics Provides Insights into Translation Regulation under Stress",
abstract = "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 H2O2. 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.",
keywords = "K63 ubiquitin, oxidative stress, proteomics, ribosome, translational control",
author = "Songhee Back and Gorman, {Andrew W.} and Christine Vogel and Silva, {Gustavo M.}",
year = "2018",
month = "1",
day = "1",
doi = "10.1021/acs.jproteome.8b00623",
language = "English (US)",
journal = "Journal of Proteome Research",
issn = "1535-3893",
publisher = "American Chemical Society",

}

TY - JOUR

T1 - Site-Specific K63 Ubiquitinomics Provides Insights into Translation Regulation under Stress

AU - Back, Songhee

AU - Gorman, Andrew W.

AU - Vogel, Christine

AU - Silva, Gustavo M.

PY - 2018/1/1

Y1 - 2018/1/1

N2 - 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 H2O2. 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.

AB - 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 H2O2. 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.

KW - K63 ubiquitin

KW - oxidative stress

KW - proteomics

KW - ribosome

KW - translational control

UR - http://www.scopus.com/inward/record.url?scp=85058522163&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85058522163&partnerID=8YFLogxK

U2 - 10.1021/acs.jproteome.8b00623

DO - 10.1021/acs.jproteome.8b00623

M3 - Article

C2 - 30489083

AN - SCOPUS:85058522163

JO - Journal of Proteome Research

JF - Journal of Proteome Research

SN - 1535-3893

ER -