488
Chaperones, Molecular
5
Chaperones and Cellular Processes
508
5.1
Chaperones and Redox Potential
508
5.1.1
Disulfde Bond Formation and Isomerization in Prokaryotes
and Eukaryotes
508
5.1.2
Hsp33: A Chaperone with a Redox Switch
510
5.2
Chaperone Networks and Protein Quality Control in the Cell
511
5.2.1
Chaperone Networks and Protein Quality Control in the
E. coli
Cytosol
511
5.2.2
Protein Quality Control in the Endoplasmic Reticulum
513
5.3
Examples o± Substrate-specifc Chaperones
514
5.3.1
Hsp47 and Collagen Assembly
514
5.3.2
PapD and the Assembly o± Bacterial Pili
515
6
Conclusion
516
Acknowledgments
517
Bibliography
517
Books and Reviews
517
Primary Literature
517
Keywords
Chaperonin
One o± a member o± the ±amily o± molecular chaperones that are homologous to the
E. coli
GroEL chaperone, and the mitochondrial and chloroplast Hsp60 chaperones.
Cochaperone
A protein that, while not possessing intrinsic chaperone properties itsel±, is required
±or a particular chaperone to ±unction.
Heat Shock
The exposure o± cells or organisms to temperatures a ±ew degrees above their normal
growth temperature, widely used as an experimental model ±or inducing cellular stress.
HSP
Abbreviation ±or ‘‘heat shock protein.’’ HSPs are proteins that are induced
de novo
or
are upregulated as a result o± heat shock.
Molecular Chaperone
Proteins that assist other proteins to reach their fnal active con±ormation, but that are
not themselves part o± this fnal con±ormation.
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