Chaperones, Chaperonin and Heat‐Shock Proteins

The protein folding of a nascent polypeptide is the decoding of the linear information contained in the primary sequence into the native three-dimensional conformation. Chaperone proteins and folding catalysts may contribute to successful folding.

Keywords: protein folding; chaperones; folding catalysts

Figure 1. Modular organization of the domains in protein disulfide isomerase-related proteins. a, a’ are the two redox-active domains, which are separated by the two thioredoxin-related domains, b, b’. Fragment c may be involved in the recognition and binding of polypeptides.
Figure 2. Isomerization of peptide bonds. (a) The steric hindrance around the amide bond favours the trans-conformation of a peptide bond. (b) cistrans isomerization of a peptidyl–prolyl bond.
Figure 3. Basic mechanism of E. coli GroEL-GroES assisted folding. The vertical section of GroEL double ring shows the apical (A), intermediate (I) and equatorial (E) domains. U, unfolded polypeptide; N, native protein.
Figure 4. Basic mechanism of E. coli Dna K assisted folding. K, Dna K; J, Dna J; S, substrate peptide; GrpE, nucleotide-exchange factor.
close
 References
    Anfinsen CB (1973) Principles that govern the folding of protein chains. Science 181: 223–230.
    Buchner J (1999) Hsp90 & Co – a holding for folding. Trends in Biochemical Sciences 24: 136–141.
    Daggett V and Fersht AR (2003) Is there a unifying mechanism for protein folding?. Trends in Biochemical Sciences 28: 18–25.
    Dobson CM (1999) Protein misfolding, evolution and disease. Trends in Biochemical Sciences 24: 329–332.
    book Dobson CM (2000) "The nature and significance of protein folding". In: Pain RH (ed.) Mechanisms of Protein Folding, 2nd edn, pp. 1–33. Oxford: IRL Press.
    Dobson CM (2002) Getting out of shape. Nature 418: 729–730.
    Ellis RJ (2001) Macromolecular crowding: an important but neglected aspect of the intracellular environment. Current Opinion in Structural Biology 11: 114–119.
    Ferrari DM and Söling HD (1999) The protein disulphide-isomerase family: unravelling a string of folds. Biochemical Journal 339: 1–10.
    Göthel SF and Marahiel MA (1999) Peptidyl-prolyl cis–trans isomerases, a superfamily of ubiquitous folding catalysts. Cellular and Molecular Life Sciences 55: 423–436.
    Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381: 571–580.
    Hartl FU and Hayer-Hartl M (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295: 1852–1858.
    ePath http://archive.bmn.com/supp/tibs/saibil.html (2002) The chaperonin folding machine.
    book http://people.cryst.bbk.ac.uk/~ubcg16z/chaperone.html (2002) Molecular Chaperone Group. London: School of Crystallography, Birkbeck College.
    Jaenicke R (1999) Stability and folding of domain proteins. Progress in Biophysics and Molecular Biology 71: 155–241.
    Ranson NA, White HE and Saibil HR (1998) Chaperonins. Biochemical Journal 333: 233–242.
    Saibil HR and Ranson NA (2002) The chaperonin folding machine. Trends in Biochemical Sciences 27: 627–632.
    Schiene C and Fischer G (2000) Enzymes that catalyse the restructuring of proteins. Current Opinion in Structural Biology 10: 40–45.
    Xu Z, Horwich AL and Sigler PB (1997) The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388: 741–750.
 Further Reading
    Dobson CM (2001) The structural basis of protein folding and its links with human disease. Philosophical Transactions of the Royal Society of London Series B Biological Sciences 356: 133–145.
    Ellis RJ (1993) The general concept of molecular chaperones. Philosophical Transactions of the Royal Society of London Series B 339: 257–261.
    book Freedman RB (1992) "Protein folding in the cell". In: Creighton TE (ed.) Protein Folding, pp. 455–539. New York: Freeman.
    Frydman J (2001) Folding of newly translated proteins in vivo: the role of molecular chaperones. Annual Review of Biochemistry 70: 603–647.
    Georgopoulos C and Welch WJ (1993) Role of the major heat shock proteins as molecular chaperones. Annual Review of Cell and Developmental Biology 9: 601–634.
    book Hlodan R and Hartl FU (1994) "How the protein folds in the cell". In: Pain RH (ed.) Mechanisms of Protein Folding, pp. 194–228. Oxford: IRL Press.
    book Leroux MR and Hartl FU (2000) "Cellular function of molecular chaperones". In: Pain RH (ed.) Mechanisms of Protein Folding, 2nd edn, pp. 364–405. Oxford: IRL Press.
    Saibil HR (2000) Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins. Current Opinion in Structural Biology 10: 251–258.
    Slavotinek AM and Biesecker LG (2001) Unfolding the role of chaperones and chaperonins in human disease. Trends in Genetics 17: 528–535.
Contact Editor close
Submit a note to the editor about this article by filling in the form below.

* Required Field

How to Cite close
Consalvi, Valerio, and Chiaraluce, Roberta(Sep 2005) Chaperones, Chaperonin and Heat‐Shock Proteins. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1038/npg.els.0003886]