Proteomics

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Sod1 Integrates Oxygen Availability to Redox Regulate NADPH Production and the Thiol Redoxome

ABSTRACT: Redox proteomics identifies additional putative targets of Sod1 redox regulation. The high abundance and broad cellular distribution of Sod1 suggests that it may function as a redox regulator of a broad variety of substrates in addition to GAPDH. To test this, we conducted a high-powered quantitative redox proteomics screen of WT and sod1Δ yeast to identify Sod1-dependent redox substrates. We used a combined SILAC-TMT approach, whereby sod1Δ-dependent changes in protein abundance are quantified through Stable Isotope Labeling with Amino acids in Cell culture (SILAC) and changes in reversible cysteine oxidation are quantified through cysteine-reactive Iodoacetyl Tandem Mass Tags (iodo-TMT) before and after reduction with DTT. Consequently, the study reveals a broad range of proteins that undergo significant changes in abundance, cysteine oxidation, or both. Focusing first on the effects of SOD1 deletion on proteome-wide protein abundance, we independently analyzed the SILAC MS data. A total of 4,409 proteins were confidently detected and quantified, and ~9% of these (373) exhibited significant differences in abundance between the two strains. Of these, 114 (30.6%) exhibit a significant decrease in protein abundance in sod1Δ cells compared to 259 (69.4%) proteins that exhibit a significant increase in abundance. Overall, we revealed a larger network of cysteine-containing proteins that are oxidized in a Sod1- dependent manner using mass spectrometry-based redox proteomics approaches.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Matthew Torres  

LAB HEAD: Matthew Phillip Torres

PROVIDER: PXD030372 | Pride | 2022-01-04

REPOSITORIES: Pride

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Sod1 integrates oxygen availability to redox regulate NADPH production and the thiol redoxome.

Montllor-Albalate Claudia C   Kim Hyojung H   Thompson Anna E AE   Jonke Alex P AP   Torres Matthew P MP   Reddi Amit R AR  

Proceedings of the National Academy of Sciences of the United States of America 20220101 1

Cu/Zn superoxide dismutase (Sod1) is a highly conserved and abundant antioxidant enzyme that detoxifies superoxide (O<sub>2</sub><sup>•-</sup>) by catalyzing its conversion to dioxygen (O<sub>2</sub>) and hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>). Using <i>Saccharomyces cerevisiae</i> and mammalian cells, we discovered that a major aspect of the antioxidant function of Sod1 is to integrate O<sub>2</sub> availability to promote NADPH production. The mechanism involves Sod1-derived H<sub>2</s  ...[more]

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