Table 1.
Chaperone Family | Functions | Annotated Subcellular Localizations (UniProt [8]) * | Curated Samples and Related Proteins: UniProt [8] *,++ |
---|---|---|---|
Hsp60 | Segregate unfolded polypeptide chains Promote unfolding of misfolded polypeptides by both active and passive mechanisms |
Chloroplast Cytoplasm Mitochondria |
Prokaryotic: 60 kDa chaperonin (1–4); cpn60; groEL; groL; groL1 to groL5; mimG; prmG; thsC Eukaryotic: cpn60 (I and II; 1 and 2); groL(A and B); hsp60; Hspd1; Rubisco large subunit binding protein (alpha1, beta1, and beta2) Tcm62 |
Hsp70 | Unfold misfolded polypeptides Translocate unfolded polyproteins through membranes Dissociate protein complexes |
Chloroplast Cytoplasm Endoplasmic Reticulum (ER) Mitochondria Nucleus |
Viral: Movement protein Hsp70h Prokaryotic: Heat shock 70 kDA protein; Hsp70; chaperone protein DnaK (1–3): [Cochaperones: DnaJ; GrpE (1 and 2)] HscA: [Cochaperone: HscB] HscC; Ssa (1 and 2); SsC1 Eukaryotic: Heat shock 70 kDA protein (1, 1A, 1B, 2, 3, 4, 4L, 5–10, 12–18) Chaperone Protein DnaK [Cochaperone: DnaJ] AtHsp70- (2,4,12,13); endoplasmic reticulum chaperone: BiP (1–5, 8); heat shock 70 kDA protein cognate (1, 2, 4, 5, II, IV); Hsc70; heat shock protein 70.2; Hsp1; hypoxia upregulated protein 1 (hyou1); Lhs1 major heat shock 70 kDA protein (Aa, Ab, Ba, Bb, Bbb, Bb); Sse (1 and 2); SsA (1–3); SsB1; SsC (1, 3); SsQ1; Sce70 |
Hsp90 | Modification of kinases, steroid hormone receptors, and transcription factors | Cytoplasm Endoplasmic Reticulum (ER) Mitochondria Nucleus |
Prokaryotic: Chaperone protein HtpG Eukaryotic: ATP-dependent molecular chaperone Hsc82; endoplasmin; endoplasmin homologs (Lpg3, Hsp90-7, grp94); heat shock cognate protein 80; heat shock-like 85 kDa protein; heat shock protein 81 (1–3); Hsp83; Hsp90 (1-6, alpha, A2, beta): [Cochaperones: Aha1; AHSA2P (putative); Cdc37; Cdc37-like 1; daf-41; Hch1; Hsp interacting protein, HIP; p23 (1, 2); PhPL3; peptidyl-prolyl cis trans isomerases (PPID, FKBP (4, 5, 8, 62, 65)); Protein canopy homolog 3; protein disulfide isomerase (PDI-A2, A4, A6); PPP5C; Sba1; Sgt (a, 1); OsSGT1, AtSgt1; Shu; Unc45-A,B (potential); wos2; Mod-E; Swo1 |
Hsp104 | Dissociation, refolding, and resolubilization of protein aggregates [8] | Cytoplasm Nucleus |
Eukaryotic: ClpB1 Hsp104 |
* Table 1 summarizes available data in the UniProt database for the different chaperone families discussed in the paper. Examples of these chaperones, their co-chaperones, and cellular locations are given. The results shown are from the entries curated as “Reviewed” by UniProt [8]. Other entries may have been added to the list since the manuscript was written. ++ Brackets denote cochaperones of the previously listed chaperone protein. Example: DnaK: [Cochaperone: DnaJ].