Proteomics

Dataset Information

0

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

Json Xml

Dataset's files

Source:
Action DRS
P10_SOD1_2019_10_14_SILAC_TMT_1_3_NCE_28_SILAC.msf Msf
P10_SOD1_2019_10_14_SILAC_TMT_1_3_NCE_28_SILAC.msfView Msf
P10_SOD1_2019_10_14_SILAC_TMT_1_3_NCE_28_SILAC.pdResult Other
P10_SOD1_2019_10_14_SILAC_TMT_1_3_NCE_28_SILAC.pdResultView Other
P10_SOD1_2019_10_14_SILAC_TMT_1_3_NCE_28_TMT.msf Msf
Items per page:
1 - 5 of 342
altmetric image

Publications

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]

Similar Datasets

Proteomics Characterization of the redox proteome of Drosophila melanogaster S2 cells and w1118 fly eyes.
2023-04-27 | PXD034050 | Pride
Proteomics Characterization of the redox proteome in Drosophila melanogaster aging eyes.
2023-04-27 | PXD036110 | Pride
Proteomics Redox regulation of cytosolic translation in rice during fungal infection identified by quantitative proteomics
2023-06-06 | PXD034430 | Pride
Transcriptomics Profiling oxidative stress in Saccharomyces cerevisiae by oxidation of transcription factor Swi6p
2011-01-31 | E-GEOD-18334 | biostudies-arrayexpress
Genomics Analysis of SOD1 binding sites by next generation sequencing under different redox environments
2018-12-20 | GSE124082 | GEO
Transcriptomics In vivo assessment of ROS production and oxidative stress effects induced by chronic exposure to gamma radiation in C. elegans
2019-10-17 | E-MTAB-8284 | biostudies-arrayexpress
Proteomics Quantitative analysis of redox proteome reveals protein thiol switches regulating fundamental processes in developmental haematopoiesis
2022-06-09 | PXD030043 | Pride
Proteomics Comprehensive redox profiling of the thiol proteome of Clostridium difficile
2018-03-05 | PXD007278 | Pride
Proteomics Quantitative profiling of protein sulfhydrome by the BTA-TMT
2020-03-09 | PXD015307 | Pride
Proteomics We applied an iodoacetyl tandem mass tags (iodoTMT)-based proteomic approach to analyze the redox proteome of Brassica napus seedlings under control and salt-stressed conditions. We identified 1,821 sulfenylated sites in 912 proteins from all samples.
2021-08-18 | PXD027721 | Pride