PXD030372

PXD030372 is an original dataset announced via ProteomeXchange.

Title	Sod1 Integrates Oxygen Availability to Redox Regulate NADPH Production and the Thiol Redoxome
Description	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.
HostingRepository	PRIDE
AnnounceDate	2024-10-07
AnnouncementXML	Submission_2024-10-07_13:44:15.161.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Matthew Torres
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	TMT6plex-126 reporter+balance reagent acylated residue; 6x(13)C; acetylated residue; monohydroxylated residue
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2021-12-13 10:09:20	ID requested
⏵ 1	2024-10-07 13:44:16	announced

10.1073/pnas.2023328119;

Montllor-Albalate C, Kim H, Thompson AE, Jonke AP, Torres MP, Reddi AR, Sod1 integrates oxygen availability to redox regulate NADPH production and the thiol redoxome. Proc Natl Acad Sci U S A, 119(1):(2022) [pubmed]

submitter keyword: pentose phosphate pathway, superoxide dismutase,oxygen sensing, redox signailng, glycolysis

Matthew Phillip Torres
contact affiliation	School of Biological Sciences, Georgia Institute of Technology, Atlanta, GA 30332
contact email	mtorres35@gatech.edu
lab head
Matthew Torres
contact affiliation	Georgia Institute of Technology
contact email	mtorres35@gatech.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD030372
     1. Label: PRIDE project
     2. Name: Sod1 Integrates Oxygen Availability to Redox Regulate NADPH Production and the Thiol Redoxome