FOG01705
EOG8VHHS8
sce:TSA1
Genes: 31
SGD DescriptionThioredoxin 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
PomBase Descriptionthioredoxin peroxidase Tpx1
References
Kim K, et al. (1988 Apr 5). The isolation and purification of a specific "protector" protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-function oxidation system.
Chae HZ, et al. (1993 Aug 5). Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae.
Chae HZ, et al. (1994 Jul 19). Dimerization of thiol-specific antioxidant and the essential role of cysteine 47.
Chae HZ, et al. (1994 Nov 4). Thioredoxin-dependent peroxide reductase from yeast.
Jeong JS, et al. (1999 Jan 12). Purification and characterization of a second type thioredoxin peroxidase (type II TPx) from Saccharomyces cerevisiae.
Park SG, et al. (2000 Feb 25). Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae.
Urban C, et al. (2003 Jun 5). Identification of cell surface determinants in Candida albicans reveals Tsa1p, a protein differentially localized in the cell.
Biteau B, et al. (2003 Oct 30). ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin.
Munhoz DC, et al. (2004 Aug 20). Cytosolic thioredoxin peroxidase I and II are important defenses of yeast against organic hydroperoxide insult: catalases and peroxiredoxins cooperate in the decomposition of H2O2 by yeast.
Jang HH, et al. (2004 May 28). Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function.
Shin DH, et al. (2005 Aug). Characterization of thiol-specific antioxidant 1 (TSA1) of Candida albicans.
Okazaki S, et al. (2005 Mar-Apr). Peroxiredoxin-mediated redox regulation of the nuclear localization of Yap1, a transcription factor in budding yeast.
Urban C, et al. (2005 Sep). The moonlighting protein Tsa1p is implicated in oxidative stress response and in cell wall biogenesis in Candida albicans.
Trotter EW, et al. (2008 May 15). The yeast Tsa1 peroxiredoxin is a ribosome-associated antioxidant.
Tachibana T, et al. (2009 Feb 13). A major peroxiredoxin-induced activation of Yap1 transcription factor is mediated by reduction-sensitive disulfide bonds and reveals a low level of transcriptional activation.
Starita LM, et al. (2012 Jan). Sites of ubiquitin attachment in Saccharomyces cerevisiae.
Tairum CA Jr, et al. (2012 Nov 23). Disulfide biochemistry in 2-cys peroxiredoxin: requirement of Glu50 and Arg146 for the reduction of yeast Tsa1 by thioredoxin.
Weids AJ, et al. (2014 Mar 15). The yeast peroxiredoxin Tsa1 protects against protein-aggregate-induced oxidative stress.
FOG01706
EOG8VHHS8
sce:TSA2
Genes: 1
SGD DescriptionStress inducible cytoplasmic thioredoxin peroxidase; cooperates with Tsa1p in the removal of reactive oxygen, nitrogen and sulfur species using thioredoxin as hydrogen donor; deletion enhances the mutator phenotype of tsa1 mutants; protein abundance increases in response to DNA replication stress; TSA2 has a paralog, TSA1, that arose from the whole genome duplication
References
Jeong JS, et al. (1999 Jan 12). Purification and characterization of a second type thioredoxin peroxidase (type II TPx) from Saccharomyces cerevisiae.
Park SG, et al. (2000 Feb 25). Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae.
Wong CM, et al. (2002 Feb 15). Cooperation of yeast peroxiredoxins Tsa1p and Tsa2p in the cellular defense against oxidative and nitrosative stress.
Munhoz DC, et al. (2004 Aug 20). Cytosolic thioredoxin peroxidase I and II are important defenses of yeast against organic hydroperoxide insult: catalases and peroxiredoxins cooperate in the decomposition of H2O2 by yeast.
Jang HH, et al. (2004 May 28). Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function.
Nielsen MH, et al. (2016 Jan). Structure of TSA2 reveals novel features of the active-site loop of peroxiredoxins.