J domain-containing protein APJ1; Chaperone with a role in SUMO-mediated protein degradation; member of the DnaJ-like family; conserved across eukaryotes; overexpression interferes with propagation of the [Psi+] prion; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; forms nuclear foci upon DNA replication stress.

ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication.

J domain-containing protein APJ1; Chaperone with a role in SUMO-mediated protein degradation; member of the DnaJ-like family; conserved across eukaryotes; overexpression interferes with propagation of the [Psi+] prion; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; forms nuclear foci upon DNA replication stress.

Trimeric heat shock transcription factor; activates multiple genes in response to highly diverse stresses; recognizes variable heat shock elements (HSEs) consisting of inverted NGAAN repeats; monitors translational status of cell through an RQC (Ribosomal Quality Control)-mediated translation-stress signal; involved in diauxic shift; posttranslationally regulated; human homolog HSF1 with linker region mutations can complement yeast hsf1 mutant; Belongs to the HSF family.

J domain-containing protein APJ1; Chaperone with a role in SUMO-mediated protein degradation; member of the DnaJ-like family; conserved across eukaryotes; overexpression interferes with propagation of the [Psi+] prion; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; forms nuclear foci upon DNA replication stress.

ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication.

J domain-containing protein APJ1; Chaperone with a role in SUMO-mediated protein degradation; member of the DnaJ-like family; conserved across eukaryotes; overexpression interferes with propagation of the [Psi+] prion; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; forms nuclear foci upon DNA replication stress.

Protein SIS1; Type II HSP40 co-chaperone that interacts with the HSP70 protein Ssa1p; shuttles between cytosol and nucleus; mediates delivery of misfolded proteins into the nucleus for degradation; involved in proteasomal degradation of misfolded cytosolic proteins; protein abundance increases in response to DNA replication stress; polyQ aggregates sequester Sis1p and interfere with clearance of misfolded proteins; similar to bacterial DnaJ proteins and mammalian DnaJB1.

J domain-containing protein APJ1; Chaperone with a role in SUMO-mediated protein degradation; member of the DnaJ-like family; conserved across eukaryotes; overexpression interferes with propagation of the [Psi+] prion; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; forms nuclear foci upon DNA replication stress.

Heat shock protein SSA1; ATPase involved in protein folding and NLS-directed nuclear transport; member of HSP70 family; required for ubiquitin-dependent degradation of short-lived proteins; forms chaperone complex with Ydj1p; localized to nucleus, cytoplasm, cell wall; 98% identical to paralog Ssa2p with different functional specificity in propagation of yeast [URE3] prions, vacuolar-mediated degradations of gluconeogenesis enzymes; general targeting factor of Hsp104p to prion fibrils.

J domain-containing protein APJ1; Chaperone with a role in SUMO-mediated protein degradation; member of the DnaJ-like family; conserved across eukaryotes; overexpression interferes with propagation of the [Psi+] prion; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; forms nuclear foci upon DNA replication stress.

Heat shock protein SSA2; HSP70 family ATP-binding protein; involved in protein folding, vacuolar import of proteins; required for ubiquitin-dependent degradation of short-lived proteins; associated with chaperonin-containing T-complex; 98% identical to paralog Ssa1p with distinct functional specificity in propagation of yeast [URE3] prions and vacuolar-mediated degradation of gluconeogenesis enzymes; binds tRNA, has role in tRNA nuclear import during starvation.

J domain-containing protein APJ1; Chaperone with a role in SUMO-mediated protein degradation; member of the DnaJ-like family; conserved across eukaryotes; overexpression interferes with propagation of the [Psi+] prion; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; forms nuclear foci upon DNA replication stress.

Heat shock protein SSA3; ATPase involved in protein folding and the response to stress; plays a role in SRP-dependent cotranslational protein-membrane targeting and translocation; member of the heat shock protein 70 (HSP70) family; localized to the cytoplasm; SSA3 has a paralog, SSA4, that arose from the whole genome duplication.

J domain-containing protein APJ1; Chaperone with a role in SUMO-mediated protein degradation; member of the DnaJ-like family; conserved across eukaryotes; overexpression interferes with propagation of the [Psi+] prion; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; forms nuclear foci upon DNA replication stress.

Heat shock protein that is highly induced upon stress; plays a role in SRP-dependent cotranslational protein-membrane targeting and translocation; member of the HSP70 family; cytoplasmic protein that concentrates in nuclei upon starvation; SSA4 has a paralog, SSA3, that arose from the whole genome duplication.

J domain-containing protein APJ1; Chaperone with a role in SUMO-mediated protein degradation; member of the DnaJ-like family; conserved across eukaryotes; overexpression interferes with propagation of the [Psi+] prion; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; forms nuclear foci upon DNA replication stress.

Cytoplasmic ATPase that is a ribosome-associated molecular chaperone; functions with J-protein partner Zuo1p; may be involved in folding of newly-made polypeptide chains; member of the HSP70 family; interacts with phosphatase subunit Reg1p; SSB1 has a paralog, SSB2, that arose from the whole genome duplication; Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily.

J domain-containing protein APJ1; Chaperone with a role in SUMO-mediated protein degradation; member of the DnaJ-like family; conserved across eukaryotes; overexpression interferes with propagation of the [Psi+] prion; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; forms nuclear foci upon DNA replication stress.

Cytoplasmic ATPase that is a ribosome-associated molecular chaperone; functions with J-protein partner Zuo1p; may be involved in the folding of newly-synthesized polypeptide chains; member of the HSP70 family; SSB2 has a paralog, SSB1, that arose from the whole genome duplication; Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily.

J domain-containing protein APJ1; Chaperone with a role in SUMO-mediated protein degradation; member of the DnaJ-like family; conserved across eukaryotes; overexpression interferes with propagation of the [Psi+] prion; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; forms nuclear foci upon DNA replication stress.

Heat shock protein STI1; Hsp90 cochaperone; regulates spatial organization of amyloid-like proteins in the cytosol, thereby buffering the proteotoxicity caused by amyloid-like proteins; interacts with the Ssa group of the cytosolic Hsp70 chaperones and activates Ssa1p ATPase activity; interacts with Hsp90 chaperones and inhibits their ATPase activity; homolog of mammalian Hop.

J domain-containing protein APJ1; Chaperone with a role in SUMO-mediated protein degradation; member of the DnaJ-like family; conserved across eukaryotes; overexpression interferes with propagation of the [Psi+] prion; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; forms nuclear foci upon DNA replication stress.

Mitochondrial protein import protein MAS5; Type I HSP40 co-chaperone; involved in regulation of HSP90 and HSP70 functions; acts as an adaptor that helps Rsp5p recognize cytosolic misfolded proteins for ubiquitination after heat shock; critical for determining cell size at Start as a function of growth rate; involved in protein translocation across membranes; member of the DnaJ family; chimeric protein in which human p58IPK J domain replaces yeast Ydj1p J domain can complement yeast ydj1 mutant.

Histone chaperone ASF1; Nucleosome assembly factor; involved in chromatin assembly, disassembly; required for recovery after DSB repair; role in H3K56 acetylation required for expression homeostasis, buffering mRNA synthesis rate against gene dosage changes in S phase; anti-silencing protein, derepresses silent loci when overexpressed; role in regulating Ty1 transposition; relocalizes to cytosol under hypoxia; growth defect of asf1 null is functionally complemented by either human ASF1A or ASF1B.

Catalytic subunit of the histone acetyltransferase complex (NuA4); acetylates four conserved internal lysines of histone H4 N-terminal tail and can acetylate histone H2A; master regulator of cellular acetylation balance; required for cell cycle progression and transcriptional silencing at the rDNA locus and regulation of autophagy; human ortholog TIP60/KAT5 is implicated in cancer and other diseases, functionally complements lethality of the esa1 null mutation.

Histone chaperone ASF1; Nucleosome assembly factor; involved in chromatin assembly, disassembly; required for recovery after DSB repair; role in H3K56 acetylation required for expression homeostasis, buffering mRNA synthesis rate against gene dosage changes in S phase; anti-silencing protein, derepresses silent loci when overexpressed; role in regulating Ty1 transposition; relocalizes to cytosol under hypoxia; growth defect of asf1 null is functionally complemented by either human ASF1A or ASF1B.

Histone deacetylase HDA1; Putative catalytic subunit of a class II histone deacetylase complex; role in azole resistance via Hsp90p, and in the heat shock response; Hda1p interacts with the Hda2p-Hda3p subcomplex to form an active tetramer; deletion increases histone H2B, H3 and H4 acetylation; other members of the HDA1 histone deacetylase complex are Hda2p and Hda3p.

Histone chaperone ASF1; Nucleosome assembly factor; involved in chromatin assembly, disassembly; required for recovery after DSB repair; role in H3K56 acetylation required for expression homeostasis, buffering mRNA synthesis rate against gene dosage changes in S phase; anti-silencing protein, derepresses silent loci when overexpressed; role in regulating Ty1 transposition; relocalizes to cytosol under hypoxia; growth defect of asf1 null is functionally complemented by either human ASF1A or ASF1B.

Protein HIR1; Subunit of the HIR complex; HIR is a nucleosome assembly complex involved in regulation of histone gene transcription; contributes to nucleosome formation, heterochromatic gene silencing, and formation of functional kinetochores.

Histone chaperone ASF1; Nucleosome assembly factor; involved in chromatin assembly, disassembly; required for recovery after DSB repair; role in H3K56 acetylation required for expression homeostasis, buffering mRNA synthesis rate against gene dosage changes in S phase; anti-silencing protein, derepresses silent loci when overexpressed; role in regulating Ty1 transposition; relocalizes to cytosol under hypoxia; growth defect of asf1 null is functionally complemented by either human ASF1A or ASF1B.

Histone transcription regulator 3; Subunit of the HIR complex; a nucleosome assembly complex involved in regulation of histone gene transcription; involved in position-dependent gene silencing and nucleosome reassembly; ortholog of human CABIN1 protein.

Histone chaperone ASF1; Nucleosome assembly factor; involved in chromatin assembly, disassembly; required for recovery after DSB repair; role in H3K56 acetylation required for expression homeostasis, buffering mRNA synthesis rate against gene dosage changes in S phase; anti-silencing protein, derepresses silent loci when overexpressed; role in regulating Ty1 transposition; relocalizes to cytosol under hypoxia; growth defect of asf1 null is functionally complemented by either human ASF1A or ASF1B.

Histone promoter control protein 2; Subunit of the HIR complex; HIR is a nucleosome assembly complex involved in regulation of histone gene transcription; mutants display synthetic defects with subunits of FACT, a complex that allows passage of RNA Pol II through nucleosomes.

Histone chaperone ASF1; Nucleosome assembly factor; involved in chromatin assembly, disassembly; required for recovery after DSB repair; role in H3K56 acetylation required for expression homeostasis, buffering mRNA synthesis rate against gene dosage changes in S phase; anti-silencing protein, derepresses silent loci when overexpressed; role in regulating Ty1 transposition; relocalizes to cytosol under hypoxia; growth defect of asf1 null is functionally complemented by either human ASF1A or ASF1B.

Conserved NAD+ dependent histone deacetylase of the Sirtuin family; deacetylation targets are primarily nuclear proteins; required for telomere hypercluster formation in quiescent yeast cells; involved in regulation of lifespan; plays roles in silencing at HML, HMR, telomeres, and rDNA; negatively regulates initiation of DNA replication; functions as regulator of autophagy like mammalian homolog SIRT1, and also of mitophagy.

Histone chaperone ASF1; Nucleosome assembly factor; involved in chromatin assembly, disassembly; required for recovery after DSB repair; role in H3K56 acetylation required for expression homeostasis, buffering mRNA synthesis rate against gene dosage changes in S phase; anti-silencing protein, derepresses silent loci when overexpressed; role in regulating Ty1 transposition; relocalizes to cytosol under hypoxia; growth defect of asf1 null is functionally complemented by either human ASF1A or ASF1B.

Serine/threonine-protein kinase TEL1; Protein kinase primarily involved in telomere length regulation; contributes to cell cycle checkpoint control in response to DNA damage; acts with Red1p and Mec1p to promote interhomolog recombination by phosphorylation of Hop1; functionally redundant with Mec1p; regulates P-body formation induced by replication stress; homolog of human ataxia-telangiectasia mutated (ATM) gene.

Copper chaperone for superoxide dismutase Sod1p; involved in oxidative stress protection; Met-X-Cys-X2-Cys motif within N-terminus is involved in insertion of copper into Sod1p under conditions of copper deprivation; required for regulation of yeast copper genes in response to DNA-damaging agents; protein abundance increases in response to DNA replication stress; human homolog CCS can complement yeast ccs1 null mutant; Belongs to the CCS1 family.

Cytochrome c isoform 2, expressed under hypoxic conditions; also known as iso-2-cytochrome c; electron carrier of the mitochondrial intermembrane space that transfers electrons from ubiquinone-cytochrome c oxidoreductase to cytochrome c oxidase during cellular respiration; protein abundance increases in response to DNA replication stress; CYC7 has a paralog, CYC1, that arose from the whole genome duplication.