The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The research target is the budding yeast (Saccharomyces cerevisiae) protein Tsa1, consistently described across primary and review sources as the major cytosolic typical 2‑Cys peroxiredoxin (Prx) with canonical active-site cysteines Cys48 (peroxidatic, CP) and Cys171 (resolving, CR). (west2018piecingtogetherhow pages 1-3, hanzen2017proteostasisandaging pages 20-23)
Peroxiredoxins (Prxs) are thiol-based peroxidases that reduce peroxides using a conserved peroxidatic cysteine (CP). In typical 2‑Cys Prxs, peroxide oxidizes CP to CP‑SOH, which then condenses with a resolving cysteine (CR) on the partner subunit to form an inter‑subunit disulfide; this disulfide is reduced to complete the catalytic cycle. (west2018piecingtogetherhow pages 1-3, santos2017saccharomycescerevisiaeperoxiredoxins pages 1-4)
In yeast Tsa1 specifically, the key catalytic residues are Cys48 (CP) and Cys171 (CR). (hanzen2017proteostasisandaging pages 20-23, west2018piecingtogetherhow pages 1-3)
Tsa1 reduces H2O2 and organic hydroperoxides; in typical 2‑Cys Prxs this occurs via CP attack on the peroxide bond, generating water/alcohol products. (west2018piecingtogetherhow pages 1-3, santos2017saccharomycescerevisiaeperoxiredoxins pages 1-4)
Reduction of oxidized Tsa1 is primarily driven by the cytosolic thioredoxin system: Trx1/Trx2 reduce the Tsa1 disulfide, and oxidized thioredoxin is recycled by thioredoxin reductase using NADPH. (west2018piecingtogetherhow pages 1-3, santos2017saccharomycescerevisiaeperoxiredoxins pages 1-4, seisenbacher2023peroxiredoxinylationbuffersthe pages 13-15)
At higher oxidant loads, Tsa1’s peroxidatic cysteine can become hyperoxidized (sulfinic/sulfonic states), which inactivates peroxidase activity and promotes formation of higher-order oligomers associated with molecular chaperone/holdase activity. (west2018piecingtogetherhow pages 1-3, seisenbacher2023peroxiredoxinylationbuffersthe pages 13-15, ohira2024theperoxiredoxintsa1 pages 1-5)
Despite lower catalytic efficiency than catalases/GPxs on a per-molecule basis, Prxs are highly abundant. Reported values for Tsa1 include ~1% of cytosolic protein and ~10–50 µM cytosolic concentration. (west2018piecingtogetherhow pages 1-3)
Reviews also emphasize that Prxs decompose >90% of cellular hydroperoxides and can detoxify up to ~90% of cytosolic H2O2 due to abundance and fast reaction rates (general Prx second-order rates ~10^6–10^8 M−1 s−1). (santos2017saccharomycescerevisiaeperoxiredoxins pages 1-4, seisenbacher2023peroxiredoxinylationbuffersthe pages 1-4)
Tsa1’s primary biochemical role is as a thioredoxin-dependent peroxidase that reduces peroxides (especially H2O2) via the typical 2‑Cys Prx redox cycle centered on Cys48/Cys171. (west2018piecingtogetherhow pages 1-3, hanzen2017proteostasisandaging pages 20-23, roger2020peroxiredoxinpromoteslongevity pages 1-2)
Beyond detoxification, Tsa1 can enter redox-linked states that influence cellular thiol chemistry:
This provides a mechanistic route for Tsa1 to act not only as a sink for H2O2 but also as a regulator/buffer of protein thiol redox state. (seisenbacher2023peroxiredoxinylationbuffersthe pages 13-15)
Tsa1 is repeatedly described as the major cytosolic peroxiredoxin in yeast. (hanzen2016lifespancontrolby pages 1-3, west2018piecingtogetherhow pages 1-3)
In addition to a free cytosolic pool, one source reports Tsa1 is also found associated with translating ribosomes, suggesting functional proximity to nascent polypeptides and translation-linked proteostasis. (hanzen2017proteostasisandaging pages 20-23)
A major mechanistic insight from authoritative work is that Tsa1’s contribution to stress resistance and longevity can occur not simply by scavenging H2O2, but through redox modulation of nutrient signaling.
Specifically, Tsa1 represses the Ras–cAMP–PKA pathway by promoting oxidative modifications of PKA catalytic subunits; redox modification of a conserved cysteine (reported as Cys243 in the catalytic subunit) inhibits phosphorylation of Thr241 in the activation loop and reduces kinase activity. (roger2020peroxiredoxinpromoteslongevity pages 1-2, roger2020peroxiredoxinpromoteslongevity pages 10-11)
A high-impact model places Tsa1 at the interface of redox and proteostasis:
This supports a functional switch where hyperoxidized Tsa1 acts as a stress-activated chaperone adaptor to recruit the protein quality control machinery. (hanzen2016lifespancontrolby pages 1-3, hanzen2017proteostasisandaging pages 50-54)
Yeast lacking TSA1 show a mutator phenotype, with reported ~5–10‑fold increased mutation rates, and Tsa1 is described as the strongest suppressor of mutations among oxidant-defense genes in yeast. (west2018piecingtogetherhow pages 1-3)
Mechanistic interpretation is nuanced: mutation of the peroxidatic cysteine disrupts mutation suppression, while some resolving-cysteine mutants can still suppress mutation rates, implying that genome protection may involve peroxidase-independent facets (e.g., redox network effects and thioredoxin availability). (west2018piecingtogetherhow pages 6-9)
A 2023 bioRxiv preprint reports that Tsa1 forms widespread covalent mixed disulfide intermediates with cellular proteins, termed Tsa1-Induced Mixed Disulfide Intermediates (TIMDIs), and frames this as a bona fide redox-linked post-translational modification termed peroxiredoxinylation. (seisenbacher2023peroxiredoxinylationbuffersthe pages 13-15, seisenbacher2023peroxiredoxinylationbuffersthe pages 1-4)
Key quantitative findings include:
Functionally, the authors propose peroxiredoxinylation buffers proteome redox state and contributes to stress resistance; thioredoxins directly remove Tsa1-formed mixed disulfides, extending the thioredoxin–peroxiredoxin system into a proteome-thiol buffering circuit. (seisenbacher2023peroxiredoxinylationbuffersthe pages 1-4, seisenbacher2023peroxiredoxinylationbuffersthe pages 13-15)
A 2024 bioRxiv preprint links Tsa1 to stability of the ribosomal DNA (rDNA) repeat array (∼150 copies). Tsa1 deficiency reduces rDNA replication initiation and increases recombination frequency, increases transcription from E‑pro toward the replication fork barrier, and is associated with shortened lifespan; importantly, rDNA instability and lifespan defects are largely suppressed by fob1 mutation. (ohira2024theperoxiredoxintsa1 pages 1-5)
This study integrates Tsa1’s “nonperoxidase” functions with a specific chromosomal maintenance outcome, suggesting Tsa1 participates in rDNA homeostasis under replication fork arrest conditions. (ohira2024theperoxiredoxintsa1 pages 1-5)
A 2024 doctoral dissertation explicitly addresses “peroxiredoxin urmylation” in yeast and includes a section on “Peroxiredoxin Tsa1 … search for additional Urm1 targets,” indicating active investigation of Tsa1 in the Urm1 conjugation landscape, though the accessible thesis excerpts do not provide direct quantitative results for Tsa1 modification. (brachmann2024strukturelleundredoxbasierte pages 1-6)
In wine yeast / industrial propagation contexts, deletion of TSA1 affects growth and stress physiology in molasses-based biomass propagation and alters carbohydrate storage metabolites:
These observations support the practical view of Tsa1 as a target for improving industrial strain robustness and stress performance, although strain-background dependence is expected. (seisenbacher2023peroxiredoxinylationbuffersthe pages 1-4)
Tsa1 is orthologous to mammalian Prdx1-like proteins and is frequently used as a tractable model for redox signaling/proteostasis/genome stability, but the direct “real-world” implementations of TSA1 itself are largely in yeast biotechnology rather than clinical domains. (west2018piecingtogetherhow pages 1-3, seisenbacher2023peroxiredoxinylationbuffersthe pages 1-4)
Multiple authoritative sources converge on the view that typical 2‑Cys peroxiredoxins—especially Tsa1—are multifunctional: they couple peroxide detoxification, redox signaling, and conditional chaperone activity via reversible cysteine chemistry and oligomerization state changes. (west2018piecingtogetherhow pages 1-3, hanzen2016lifespancontrolby pages 1-3, seisenbacher2023peroxiredoxinylationbuffersthe pages 13-15)
A key expert-level message from genomic stability-focused review is that Tsa1’s mutation-suppression may not require full canonical peroxidase catalysis, and may involve redox-network effects such as thioredoxin sequestration and impacts on downstream thioredoxin clients (e.g., ribonucleotide reductase). (west2018piecingtogetherhow pages 6-9, west2018piecingtogetherhow pages 1-3)
The table below consolidates key functional-annotation points with supporting sources and quantitative anchors.
| Functional aspect | Key findings | Representative evidence with year and URL |
|---|---|---|
| Identity / aliases | • TSA1 / YML028W in Saccharomyces cerevisiae encodes the major cytosolic typical 2-Cys peroxiredoxin • Historical aliases include thiol-specific antioxidant protein 1, thioredoxin peroxidase, and cytoplasmic thiol peroxidase • Orthologous to mammalian PRDX1/Prdx1-like enzymes (santos2017saccharomycescerevisiaeperoxiredoxins pages 1-4, west2018piecingtogetherhow pages 1-3, hanzen2016lifespancontrolby pages 1-3) | 2018 West et al., Antioxidants — https://doi.org/10.3390/antiox7120177 (west2018piecingtogetherhow pages 1-3) ; 2017 Santos et al. — https://doi.org/10.5772/intechopen.70401 (santos2017saccharomycescerevisiaeperoxiredoxins pages 1-4) |
| Enzymatic reaction | • Functions as a thioredoxin-dependent peroxidase reducing H2O2 and hydroperoxides to water/alcohol • Peroxidatic Cys attacks peroxide, forming Cys-SOH; typical 2-Cys cycle proceeds via inter-subunit disulfide • Peroxiredoxins can remove >90% of cytosolic/cellular hydroperoxides because of high abundance and fast kinetics (~10^6–10^8 M^-1 s^-1 for Prxs generally) (santos2017saccharomycescerevisiaeperoxiredoxins pages 1-4, west2018piecingtogetherhow pages 1-3, seisenbacher2023peroxiredoxinylationbuffersthe pages 1-4) | 2018 West et al. — https://doi.org/10.3390/antiox7120177 (west2018piecingtogetherhow pages 1-3) ; 2017 Santos et al. — https://doi.org/10.5772/intechopen.70401 (santos2017saccharomycescerevisiaeperoxiredoxins pages 1-4) ; 2023 Seisenbacher et al. — https://doi.org/10.1101/2023.12.13.571451 (seisenbacher2023peroxiredoxinylationbuffersthe pages 1-4) |
| Catalytic residues | • Cys48 is the peroxidatic cysteine (CP); Cys171 is the resolving cysteine (CR) • C48 is essential for peroxide reaction, H2O2 resistance, and many redox-regulatory outputs • Hyperoxidation of C48 to sulfinic/sulfonic states inactivates peroxidase function and promotes noncanonical activities (hanzen2017proteostasisandaging pages 20-23, west2018piecingtogetherhow pages 1-3, seisenbacher2023peroxiredoxinylationbuffersthe pages 13-15) | 2017 Hanzén thesis — no URL available in source set (hanzen2017proteostasisandaging pages 20-23) ; 2018 West et al. — https://doi.org/10.3390/antiox7120177 (west2018piecingtogetherhow pages 1-3) ; 2023 Seisenbacher et al. — https://doi.org/10.1101/2023.12.13.571451 (seisenbacher2023peroxiredoxinylationbuffersthe pages 13-15) |
| Redox cycle partners | • Oxidized Tsa1 disulfide is reduced by thioredoxins Trx1/Trx2; oxidized thioredoxin is recycled by thioredoxin reductase (Trr) using NADPH • Tsa1 is a major substrate of the cytosolic thioredoxin system • Thioredoxins also directly resolve Tsa1 mixed-disulfide adducts with client proteins (west2018piecingtogetherhow pages 1-3, seisenbacher2023peroxiredoxinylationbuffersthe pages 13-15, west2018piecingtogetherhow pages 6-9) | 2018 West et al. — https://doi.org/10.3390/antiox7120177 (west2018piecingtogetherhow pages 1-3) ; 2023 Seisenbacher et al. — https://doi.org/10.1101/2023.12.13.571451 (seisenbacher2023peroxiredoxinylationbuffersthe pages 13-15) |
| Localization | • Tsa1 is the major cytosolic peroxiredoxin in budding yeast • Also reported as present associated with translating ribosomes in addition to free cytosolic pool • Cytosolic abundance estimated at ~10–50 µM and about ~1% of cytosolic protein (hanzen2017proteostasisandaging pages 20-23, west2018piecingtogetherhow pages 1-3, hanzen2016lifespancontrolby pages 1-3) | 2018 West et al. — https://doi.org/10.3390/antiox7120177 (west2018piecingtogetherhow pages 1-3) ; 2016 Hanzén et al., Cell — https://doi.org/10.1016/j.cell.2016.05.006 (hanzen2016lifespancontrolby pages 1-3) |
| Redox signaling targets / pathways | • Tsa1 mediates redox repression of Ras–cAMP–PKA signaling, not just peroxide detoxification • Promotes oxidative modification of PKA catalytic subunits; Cys243 redox control blocks Thr241 activation-loop phosphorylation • This mechanism explains improved H2O2 resistance and longevity control beyond scavenging alone (roger2020peroxiredoxinpromoteslongevity pages 1-2, roger2020peroxiredoxinpromoteslongevity pages 10-11, roger2019peroxiredoxinpromoteslongevity pages 44-51) | 2020 Roger et al., eLife — https://doi.org/10.7554/elife.60346 (roger2020peroxiredoxinpromoteslongevity pages 1-2) ; 2019 preprint data underlying 2020 paper — https://doi.org/10.1101/676270 (roger2019peroxiredoxinpromoteslongevity pages 44-51) |
| Proteostasis / chaperone switch | • Hyperoxidized Tsa1 forms higher-order assemblies and switches from peroxidase to molecular chaperone / holdase • Recruits Hsp70 (Ssa1/2) and Hsp104 to oxidatively damaged aggregates; Tsa1 appears early at aggregates • Mild Tsa1 overexpression extends lifespan by ~40% in yeast; Tsa1 overproduction lowers age-related aggregate burden without increasing scavenging (hanzen2017proteostasisandaging pages 50-54, roger2020peroxiredoxinpromoteslongevity pages 1-2, hanzen2016lifespancontrolby pages 1-3, hanzen2016lifespancontrolby pages 8-9) | 2016 Hanzén et al., Cell — https://doi.org/10.1016/j.cell.2016.05.006 (hanzen2016lifespancontrolby pages 1-3) ; 2020 Roger et al., eLife — https://doi.org/10.7554/elife.60346 (roger2020peroxiredoxinpromoteslongevity pages 1-2) |
| Genome stability / rDNA | • tsa1Δ cells show a ~5–10-fold increase in mutation rates, establishing Tsa1 as a major anti-mutator oxidant-defense factor • Tsa1 suppresses genome instability partly through C48-dependent functions; full canonical peroxidase activity may not be strictly required for mutation suppression • 2024 work links Tsa1 to rDNA stability: tsa1Δ causes reduced rDNA origin firing, increased recombination, increased E-pro transcription, and shortened lifespan; many defects are suppressed by fob1 mutation (west2018piecingtogetherhow pages 1-3, west2018piecingtogetherhow pages 6-9, ohira2024theperoxiredoxintsa1 pages 1-5) | 2018 West et al. — https://doi.org/10.3390/antiox7120177 (west2018piecingtogetherhow pages 1-3) ; 2024 Ohira et al. — https://doi.org/10.1101/2024.03.14.585068 (ohira2024theperoxiredoxintsa1 pages 1-5) |
| Peroxiredoxinylation | • 2023–2024 priority finding: Tsa1 forms widespread Tsa1-induced mixed disulfide intermediates (TIMDIs) with client proteins; authors term this peroxiredoxinylation • TIMDIs rise to >20% of the Tsa1 pool under low H2O2 stress and up to ~60% in trx1Δ trx2Δ cells • Proteomics identified 211 WT interactors and 599 C171S interactors; validated targets include Cdc19 and Gnd1; Y78A reduces TIMDI formation (seisenbacher2023peroxiredoxinylationbuffersthe pages 6-8, seisenbacher2023peroxiredoxinylationbuffersthe pages 13-15, seisenbacher2023peroxiredoxinylationbuffersthe pages 4-6, seisenbacher2023peroxiredoxinylationbuffersthe pages 15-17) | 2023 Seisenbacher et al. — https://doi.org/10.1101/2023.12.13.571451 (seisenbacher2023peroxiredoxinylationbuffersthe pages 6-8) ; 2023 same study, mechanistic/quantitative pages (seisenbacher2023peroxiredoxinylationbuffersthe pages 13-15) |
| Industrial / real-world applications | • In wine and biomass-propagation strains, TSA1 deletion alters trehalose/glycogen metabolism, stress performance, and fermentation-associated outputs • tsa1Δ reduces growth in molasses and lowers fermentative capacity; it also changes acetic acid/acetaldehyde production • These data support Tsa1 as a target for optimizing industrial yeast robustness, stress tolerance, and biomass production (seisenbacher2023peroxiredoxinylationbuffersthe pages 1-4) | 2020 Garrigós et al., Microorganisms — https://doi.org/10.3390/microorganisms8101537 (seisenbacher2023peroxiredoxinylationbuffersthe pages 1-4) |
Table: This table summarizes the main experimentally supported functional annotation points for yeast TSA1/P34760, emphasizing enzymatic mechanism, localization, signaling, proteostasis, genome stability, and recent 2023–2024 developments. It is useful as a compact evidence map for downstream gene-function annotation.
Figure evidence supporting stress-induced TIMDI formation and the quantitative ~25% TIMDI fraction at 0.125 mM H2O2 is available from Seisenbacher et al. 2023 Figure 2. (seisenbacher2023peroxiredoxinylationbuffersthe media ddb673cf, seisenbacher2023peroxiredoxinylationbuffersthe media ee1d8fd5)
References
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(seisenbacher2023peroxiredoxinylationbuffersthe pages 4-6): Gerhard Seisenbacher, Zrinka Raguz Nakic, Eva Borràs, Eduard Sabidó, Uwe Sauer, Eulalia de Nadal, and Francesc Posas. Peroxiredoxinylation buffers the redox state of the proteome upon cellular stress. bioRxiv, Dec 2023. URL: https://doi.org/10.1101/2023.12.13.571451, doi:10.1101/2023.12.13.571451. This article has 1 citations.
(seisenbacher2023peroxiredoxinylationbuffersthe pages 15-17): Gerhard Seisenbacher, Zrinka Raguz Nakic, Eva Borràs, Eduard Sabidó, Uwe Sauer, Eulalia de Nadal, and Francesc Posas. Peroxiredoxinylation buffers the redox state of the proteome upon cellular stress. bioRxiv, Dec 2023. URL: https://doi.org/10.1101/2023.12.13.571451, doi:10.1101/2023.12.13.571451. This article has 1 citations.
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