TSA1/YML028W Summary Help

Standard Name TSA1 1
Systematic Name YML028W
Alias ZRG14 2 , TPX1
Feature Type ORF, Verified
Description Thioredoxin peroxidase; acts as both a ribosome-associated and free cytoplasmic antioxidant; self-associates to form high-molecular weight chaperone complex under oxidative stress; deletion causes mutator phenotype; protein abundance increases and forms cytoplasmic foci during DNA replication stress; chaperone activity is essential for growth under zinc deficiency; required for telomere length maintenance; TSA1 has a paralog, TSA2, that arose from the whole genome duplication (1, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12)
Name Description Thiol-Specific Antioxidant 1
Gene Product Alias cTPxI
Chromosomal Location
ChrXIII:220138 to 220728 | ORF Map | GBrowse
Gene Ontology Annotations All TSA1 GO evidence and references
  View Computational GO annotations for TSA1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 13 genes
Classical genetics
gain of function
reduction of function
Large-scale survey
412 total interaction(s) for 234 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 34
  • Affinity Capture-RNA: 8
  • Affinity Capture-Western: 3
  • Biochemical Activity: 1
  • Co-crystal Structure: 2
  • Co-fractionation: 1
  • Co-purification: 3
  • PCA: 1
  • Reconstituted Complex: 3
  • Two-hybrid: 4

Genetic Interactions
  • Dosage Growth Defect: 2
  • Dosage Rescue: 3
  • Negative Genetic: 135
  • Phenotypic Enhancement: 15
  • Phenotypic Suppression: 5
  • Positive Genetic: 6
  • Synthetic Growth Defect: 115
  • Synthetic Haploinsufficiency: 1
  • Synthetic Lethality: 64
  • Synthetic Rescue: 6

Expression Summary
Length (a.a.) 196
Molecular Weight (Da) 21,590
Isoelectric Point (pI) 4.87
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXIII:220138 to 220728 | ORF Map | GBrowse
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..591 220138..220728 1996-07-31 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000004490
References cited on this page View Complete Literature Guide for TSA1
1) Chae HZ, et al.  (1993) Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae. J Biol Chem 268(22):16815-21
2) Yuan DS  (2000) Zinc-regulated genes in Saccharomyces cerevisiae revealed by transposon tagging. Genetics 156(1):45-58
3) Chae HZ, et al.  (1994) Thioredoxin-dependent peroxide reductase from yeast. J Biol Chem 269(44):27670-8
4) Wong CM, et al.  (2002) Cooperation of yeast peroxiredoxins Tsa1p and Tsa2p in the cellular defense against oxidative and nitrosative stress. J Biol Chem 277(7):5385-94
5) Huang ME, et al.  (2003) A genomewide screen in Saccharomyces cerevisiae for genes that suppress the accumulation of mutations. Proc Natl Acad Sci U S A 100(20):11529-34
6) Wong CM, et al.  (2004) Peroxiredoxin-null yeast cells are hypersensitive to oxidative stress and are genomically unstable. J Biol Chem 279(22):23207-13
7) Okazaki S, et al.  (2005) Peroxiredoxin-mediated redox regulation of the nuclear localization of Yap1, a transcription factor in budding yeast. Antioxid Redox Signal 7(3-4):327-34
8) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
9) Trotter EW, et al.  (2008) The yeast Tsa1 peroxiredoxin is a ribosome-associated antioxidant. Biochem J 412(1):73-80
10) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
11) Lu J, et al.  (2013) Deletion of the major peroxiredoxin Tsa1 alters telomere length homeostasis. Aging Cell 12(4):635-44
12) Macdiarmid CW, et al.  (2013) Peroxiredoxin Chaperone Activity Is Critical for Protein Homeostasis in Zinc-deficient Yeast. J Biol Chem 288(43):31313-27