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. 2017 Apr 12;102:367–375. doi: 10.1016/j.ijbiomac.2017.04.025

Table 1.

Components of molecular chaperones in both prokaryotic and eukaryotic cells.

Type of chaperone Classification Protein Organism Subcellar localization Functions Cooperating factors energy consumption reference
cytoplasmic HSP40 DnaJ prokaryotic (Escherichia coli) Cytosol, ER Co-chaperone [153], [154]
Hsp60 GroEL prokaryotic (Escherichia coli) Prokaryotic cytosol (Holding and Folding chaperone)
Promotes protein folding and preventing aggregation
GroES, Hspl0, Cpnl0 ATP (+) [54], [155]
Hsp58 Mammals Mitochondria
Cpn60 Plants Chloroplasts
HSP70 DnaK prokaryotic (Escherichia coli) Prokaryotic cytosol (Folding chaperone)
Assisting refolding,
Preventing aggregation, increase lysosomal degradation of cytosolic proteins, Iron-sulfur cluster protein assembly
Sigma regulation, protein translocation into ER and protein translocation into mitochondria
DnaJ, GrpE ATP (+) [156], [157]
SSA1-4 prokaryotic (Saccharomyces cerevisiae) Eukaryotic cytosol
SSB1, 2 prokaryotic (Saccharomyces cerevisiae)
Hsc73 Mammals
HscA prokaryotic (Escherichia coli) Prokaryotic cytosol
HscC
KAR2 prokaryotic (Saccharomyces cerevisiae) ER
BiP/Grp78 Mammals
SSC1 prokaryotic (Saccharomyces cerevisiae) Mitochondria
ctHsp70 Plants Chloroplasts
HSP90 HtpG prokaryotic (Escherichia coli) Prokaryotic cytosol (Holding chaperone) Assist to folding properly, make stable condition for proteins against heat stress, Regulation of receptors,
Protein translocation, Genetic buffering and protein degradation
HSP9, Grp94 ATP (+) [158], [159]
HSP90A Mammals Cytosol
HSP90B Mammals ER
TRAP Mammals Mitochondria
HSP100 Hsp104 prokaryotic (Saccharomyces cerevisiae) Mitochondria spread of yeast prions and clearance of aggregates Hsp70, DnaK, ClpP, HsIV ATP (+) [41], [160]
ClpB, C, A, X, prokaryotic (Escherichia coli) Cytosol (Disaggregated chaperones)
Fold properly and Disaggregate
Hsp78 prokaryotic (Saccharomyces cerevisiae) Mitochondria
HsIU Plants Chloroplast
sHSP GroES prokaryotic (Escherichia coli) Cytosol (Holding chaperone) Preventing aggregation during stress,
Co-chaperone, provide thermotolerance in vivo and prohibition of apoptosis
GroEL ATP (+) [76], [161]
GrpE DnaJ, DnaK
Hsp10 Humans Cytosol, mitochondria,
Chloroplast
Hsp27 Humans Cytosol, ER, Nucleus (−)
HspB6 Humans Cytosol, Nucleus
HspB1 Humans Cytosol, Nucleus



periplasmic Generic Skp (OmpH) prokaryotic (Escherichia coli) Outer membrane folding and assembling
of outer membrane proteins and
folding-assisting
(−) [93]
FkpA periplasm space
PPIases SurA prokaryotic (Escherichia coli) Outer membrane correct folding, assembly of outer membrane proteins, folding of many newly translocated proteins (−) [102], [124], [128]
PpiD
FkpA
PpiA (RotA) Humans Nucleus
disulfide bond formation DsbA prokaryotic periplasm space Folding of protein into the functional structure (−) [151], [162]
DsbB Inner membrane Cooperates with ubiquinone to generate a disulfide bond
DsbC periplasm space As a disulfide bond isomerasation and facilitate folding of the protein
DsbD Inner membrane As reductive pathway
DsbE periplasm space Facilitate folding of the protein
DsbG
Specialized SurA prokaryotic
(Escherichia coli)
Outer membrane facilitates correct folding of outer membrane proteins, (−) [99]
LolA (B,C,D,E) periplasm space, Inner membrane and Outer membrane rapid transfer of associated lipoproteins ATP (+) [108]
PapD and its family periplasm space and Outer membrane biogenesis of pilus (−) [163]
FimC periplasm space interacts with
each pilus subunit
(−) [164]