Please use this identifier to cite or link to this item: http://hdl.handle.net/1893/31863
Appears in Collections:Biological and Environmental Sciences Journal Articles
Peer Review Status: Refereed
Title: Protein structure, amino acid composition and sequence determine proteome vulnerability to oxidation-induced damage
Author(s): Chang, Roger L
Stanley, Julian A
Robinson, Matthew C
Sher, Joel W
Li, Zhanwen
Chan, Yujia A
Omdahl, Ashton R
Wattiez, Ruddy
Godzik, Adam
Matallana-Surget, Sabine
Keywords: Deinococcus radiodurans
oxidative stress
protein carbonyl
radioresistance
structural systems biology
Issue Date: 1-Dec-2020
Date Deposited: 22-Oct-2020
Citation: Chang RL, Stanley JA, Robinson MC, Sher JW, Li Z, Chan YA, Omdahl AR, Wattiez R, Godzik A & Matallana-Surget S (2020) Protein structure, amino acid composition and sequence determine proteome vulnerability to oxidation-induced damage. EMBO Journal, 39 (23), Art. No.: e104523. https://doi.org/10.15252/embj.2020104523
Abstract: Oxidative stress alters cell viability, from microorganism irradiation sensitivity to human aging and neurodegeneration. Deleterious effects of protein carbonylation by reactive oxygen species (ROS) make understanding molecular properties determining ROS susceptibility essential. The radiation‐resistant bacterium Deinococcus radiodurans accumulates less carbonylation than sensitive organisms, making it a key model for deciphering properties governing oxidative stress resistance. We integrated shotgun redox proteomics, structural systems biology, and machine learning to resolve properties determining protein damage by γ‐irradiation in Escherichia coli and D. radiodurans at multiple scales. Local accessibility, charge, and lysine enrichment accurately predict ROS susceptibility. Lysine, methionine, and cysteine usage also contribute to ROS resistance of the D. radiodurans proteome. Our model predicts proteome maintenance machinery, and proteins protecting against ROS are more resistant in D. radiodurans. Our findings substantiate that protein‐intrinsic protection impacts oxidative stress resistance, identifying causal molecular properties.
DOI Link: 10.15252/embj.2020104523
Rights: Copyright 2020 The Authors. Published under the terms of the CC BY NC ND 4.0 license (http://creativecommons.org/licenses/by-nc-nd/4.0/)
Licence URL(s): http://creativecommons.org/licenses/by-nc-nd/4.0/

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