Thioredoxin-2; Cytoplasmic thioredoxin isoenzyme; part of thioredoxin system which protects cells against oxidative and reductive stress; forms LMA1 complex with Pbi2p; acts as a cofactor for Tsa1p; required for ER-Golgi transport and vacuole inheritance; with Trx1p, facilitates mitochondrial import of small Tims Tim9p, Tim10p, Tim13p by maintaining them in reduced form; abundance increases under DNA replication stress; TRX2 has a paralog, TRX1, that arose from the whole genome duplication.

Basic leucine zipper (bZIP) transcription factor; required for oxidative stress tolerance; activated by H2O2 through the multistep formation of disulfide bonds and transit from the cytoplasm to the nucleus; Yap1p is degraded in the nucleus after the oxidative stress has passed; mediates resistance to cadmium; relative distribution to the nucleus increases upon DNA replication stress; YAP1 has a paralog, CAD1, that arose from the whole genome duplication.

Peroxiredoxin TSA1; 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; binds and modulates Cdc19p activity; protein abundance increases, forms cytoplasmic foci during DNA replication stress; TSA1 has a paralog, TSA2, that arose from the whole genome duplication; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.

Transcription factor SKN7; Nuclear response regulator and transcription factor; physically interacts with the Tup1-Cyc8 complex and recruits Tup1p to its targets; part of a branched two-component signaling system; required for optimal induction of heat-shock genes in response to oxidative stress; involved in osmoregulation; relocalizes to the cytosol in response to hypoxia; SKN7 has a paralog, HMS2, that arose from the whole genome duplication.

Mitochondrial thioredoxin reductase; involved in protection against oxidative stress, required with Glr1p to maintain the redox state of Trx3p; contains active-site motif (CAVC) present in prokaryotic orthologs; binds NADPH and FAD; TRR2 has a paralog, TRR1, that arose from the whole genome duplication.

Cytosolic and mitochondrial glutathione oxidoreductase; converts oxidized glutathione to reduced glutathione; cytosolic Glr1p is the main determinant of the glutathione redox state of the mitochondrial intermembrane space; mitochondrial Glr1p has a role in resistance to hyperoxia; protein abundance increases in response to DNA replication stress.

Mitochondrial peroxiredoxin with thioredoxin peroxidase activity; has a role in reduction of hydroperoxides; reactivation requires Trr2p and glutathione; induced during respiratory growth and oxidative stress; phosphorylated; protein abundance increases in response to DNA replication stress.

Thiol-specific peroxiredoxin; reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p; Belongs to the peroxiredoxin family. Prx5 subfamily.

Glutaredoxin-2; Cytoplasmic glutaredoxin; thioltransferase, glutathione-dependent disulfide oxidoreductase involved in maintaining redox state of target proteins, also exhibits glutathione peroxidase activity, expression induced in response to stress; GRX2 has two in-frame start codons resulting in a shorter isoform that is retained in the cytosol and a longer form translocated to the mitochondrial matrix; GRX2 has a paralog, GRX1, that arose from the whole genome duplication.