Unraveling Oxidative Stress Resistance: Molecular Properties Govern Proteome Vulnerability
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.One Sentence Summary Proteins differ in intrinsic susceptibility to oxidation, a mode of evolutionary adaptation for stress tolerance in bacteria..
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Preprint| Erscheinungsjahr: |
2020 |
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| Erschienen: |
2020 |
| Enthalten in: |
bioRxiv.org - (2020) vom: 13. März Zur Gesamtaufnahme - year:2020 |
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| Sprache: |
Englisch |
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| Beteiligte Personen: |
Chang, Roger L. [VerfasserIn] |
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| Links: |
Volltext [kostenfrei] |
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| doi: |
10.1101/2020.03.09.983213 |
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| PPN (Katalog-ID): |
XBI000800066 |
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| 520 | |a 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.One Sentence Summary Proteins differ in intrinsic susceptibility to oxidation, a mode of evolutionary adaptation for stress tolerance in bacteria. | ||
| 700 | 1 | |a Stanley, Julian A. |e verfasserin |4 aut | |
| 700 | 1 | |a Robinson, Matthew C. |e verfasserin |4 aut | |
| 700 | 1 | |a Sher, Joel W. |e verfasserin |4 aut | |
| 700 | 1 | |a Li, Zhanwen |e verfasserin |4 aut | |
| 700 | 1 | |a Chan, Yujia A. |e verfasserin |4 aut | |
| 700 | 1 | |a Omdahl, Ashton R. |e verfasserin |4 aut | |
| 700 | 1 | |a Wattiez, Ruddy |e verfasserin |4 aut | |
| 700 | 1 | |a Godzik, Adam |e verfasserin |4 aut | |
| 700 | 1 | |a Matallana-Surget, Sabine |e verfasserin |4 aut | |
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