Mass spectrometry analysis of K63-ubiquitinated targets in response to oxidative stress

Gustavo Monteiro Silva; Christine Vogel

doi:10.1016/j.dib.2015.05.002

Mass spectrometry analysis of K63-ubiquitinated targets in response to oxidative stress

Gustavo Monteiro Silva, Christine Vogel

Biology and Genomics

Research output: Contribution to journal › Article › peer-review

Abstract

The data described here provide the first large-scale analysis of lysine 63 (K63)-linked polyubiquitin targets. Protein ubiquitination is a prominent post-translational modification, and a variety of ubiquitin chains exists, serving a multitude of functions [1]. The chains differ by the lysine residue by which the ubiquitin monomers are linked. We used yeast Saccharomyces cerevisiae subjected to oxidative stress as a model to study K63 ubiquitination. K63 ubiquitinated targets were pulled-down by the K63-TUBE system (Tandem Ubiquitin Binding Entities) and analyzed by SILAC-based mass spectrometry [2]. The data are associated to the research article 'K63 polyubiquitination is a new modulator of the oxidative stress response' [3]. The mass spectrometry and the analysis dataset have been deposited to the ProteomeXchange Consortium (. http://proteomecentral.proteomexchange.org) via the PRIDE partner repository with the dataset identifier PXD000960.

Original language	English (US)
Pages (from-to)	130-134
Number of pages	5
Journal	Data in Brief
Volume	4
DOIs	https://doi.org/10.1016/j.dib.2015.05.002
State	Published - Sep 1 2015

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title = "Mass spectrometry analysis of K63-ubiquitinated targets in response to oxidative stress",

abstract = "The data described here provide the first large-scale analysis of lysine 63 (K63)-linked polyubiquitin targets. Protein ubiquitination is a prominent post-translational modification, and a variety of ubiquitin chains exists, serving a multitude of functions [1]. The chains differ by the lysine residue by which the ubiquitin monomers are linked. We used yeast Saccharomyces cerevisiae subjected to oxidative stress as a model to study K63 ubiquitination. K63 ubiquitinated targets were pulled-down by the K63-TUBE system (Tandem Ubiquitin Binding Entities) and analyzed by SILAC-based mass spectrometry [2]. The data are associated to the research article 'K63 polyubiquitination is a new modulator of the oxidative stress response' [3]. The mass spectrometry and the analysis dataset have been deposited to the ProteomeXchange Consortium (. http://proteomecentral.proteomexchange.org) via the PRIDE partner repository with the dataset identifier PXD000960.",

author = "Silva, {Gustavo Monteiro} and Christine Vogel",

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T1 - Mass spectrometry analysis of K63-ubiquitinated targets in response to oxidative stress

AU - Silva, Gustavo Monteiro

AU - Vogel, Christine

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N2 - The data described here provide the first large-scale analysis of lysine 63 (K63)-linked polyubiquitin targets. Protein ubiquitination is a prominent post-translational modification, and a variety of ubiquitin chains exists, serving a multitude of functions [1]. The chains differ by the lysine residue by which the ubiquitin monomers are linked. We used yeast Saccharomyces cerevisiae subjected to oxidative stress as a model to study K63 ubiquitination. K63 ubiquitinated targets were pulled-down by the K63-TUBE system (Tandem Ubiquitin Binding Entities) and analyzed by SILAC-based mass spectrometry [2]. The data are associated to the research article 'K63 polyubiquitination is a new modulator of the oxidative stress response' [3]. The mass spectrometry and the analysis dataset have been deposited to the ProteomeXchange Consortium (. http://proteomecentral.proteomexchange.org) via the PRIDE partner repository with the dataset identifier PXD000960.

AB - The data described here provide the first large-scale analysis of lysine 63 (K63)-linked polyubiquitin targets. Protein ubiquitination is a prominent post-translational modification, and a variety of ubiquitin chains exists, serving a multitude of functions [1]. The chains differ by the lysine residue by which the ubiquitin monomers are linked. We used yeast Saccharomyces cerevisiae subjected to oxidative stress as a model to study K63 ubiquitination. K63 ubiquitinated targets were pulled-down by the K63-TUBE system (Tandem Ubiquitin Binding Entities) and analyzed by SILAC-based mass spectrometry [2]. The data are associated to the research article 'K63 polyubiquitination is a new modulator of the oxidative stress response' [3]. The mass spectrometry and the analysis dataset have been deposited to the ProteomeXchange Consortium (. http://proteomecentral.proteomexchange.org) via the PRIDE partner repository with the dataset identifier PXD000960.

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Mass spectrometry analysis of K63-ubiquitinated targets in response to oxidative stress

Abstract

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