BAIT

TSA1

TPX1, ZRG14, thioredoxin peroxidase TSA1, cTPxI, L000002365, YML028W
Thioredoxin peroxidase; acts as both ribosome-associated and free cytoplasmic antioxidant; self-associates to form high-molecular weight chaperone complex under oxidative stress; chaperone activity essential for growth in zinc deficiency; required for telomere length maintenance; protein abundance increases, forms cytoplasmic foci during DNA replication stress; TSA1 has a paralog, TSA2, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)
PREY

TSA1

TPX1, ZRG14, thioredoxin peroxidase TSA1, cTPxI, L000002365, YML028W
Thioredoxin peroxidase; acts as both ribosome-associated and free cytoplasmic antioxidant; self-associates to form high-molecular weight chaperone complex under oxidative stress; chaperone activity essential for growth in zinc deficiency; required for telomere length maintenance; protein abundance increases, forms cytoplasmic foci during DNA replication stress; TSA1 has a paralog, TSA2, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

In vivo parameters influencing 2-Cys Prx oligomerization: The role of enzyme sulfinylation.

Noichri Y, Palais G, Ruby V, D'Autreaux B, Delaunay-Moisan A, Nystroem T, Molin M, Toledano MB

2-Cys Prxs are H2O2-specific antioxidants that become inactivated by enzyme hyperoxidation at elevated H2O2 levels. Although hyperoxidation restricts the antioxidant physiological role of these enzymes, it also allows the enzyme to become an efficient chaperone holdase. The critical molecular event allowing the peroxidase to chaperone switch is thought to be the enzyme assembly into high molecular weight (HMW) structures brought ... [more]

Redox Biol Aug. 20, 2015; 6(0);326-333 [Pubmed: 26335398]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
TSA1 TSA1
Affinity Capture-MS
Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

High-BioGRID
694698
TSA1 TSA1
Affinity Capture-MS
Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

High-BioGRID
2890777
TSA1 TSA1
Affinity Capture-Western
Affinity Capture-Western

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Low-BioGRID
3455105
TSA1 TSA1
Affinity Capture-Western
Affinity Capture-Western

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Low-BioGRID
-
TSA1 TSA1
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
345400
TSA1 TSA1
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
718414
TSA1 TSA1
Co-purification
Co-purification

An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps.

High-BioGRID
349081
TSA1 TSA1
Co-purification
Co-purification

An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps.

Low-BioGRID
-
TSA1 TSA1
Co-purification
Co-purification

An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps.

Low-BioGRID
2532659
TSA1 TSA1
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
3547681
TSA1 TSA1
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-
TSA1 TSA1
Two-hybrid
Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

High-BioGRID
-

Curated By

  • BioGRID