Proteomics

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Unraveling Oxidative Stress Resistance: Molecular Properties Govern Proteome Vulnerability


ABSTRACT: Oxidative stress leads to damage of protein molecules, particularly accumulation of protein carbonyls. 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 measured protein damage by 6.7 kGy of γ-irradiation in Escherichia coli and D. radiodurans by LC-MS/MS, and analyzed this result both to identify protein carbonyls at residue-resolution and quantifying relative abundance changes following irradiation.

ORGANISM(S): Deinococcus Radiodurans R1 Escherichia Coli

SUBMITTER: Sabine Matallana-Sur  

PROVIDER: PXD020058 | iProX | Thu Oct 22 00:00:00 BST 2020

REPOSITORIES: iProX

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Publications

Protein structure, amino acid composition and sequence determine proteome vulnerability to oxidation-induced damage.

Chang Roger L RL   Stanley Julian A JA   Robinson Matthew C MC   Sher Joel W JW   Li Zhanwen Z   Chan Yujia A YA   Omdahl Ashton R AR   Wattiez Ruddy R   Godzik Adam A   Matallana-Surget Sabine S  

The EMBO journal 20201019 23


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 sh  ...[more]

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