The chaperone function: Meanings and myths

Novartis Foundation Symposium

Volumn 291, Issue , 2008, Pages 23-36

  Lund, Peter A ^a   Ellis, R John ^b  

^a UNIVERSITY OF BIRMINGHAM   (United Kingdom)

^b UNIVERSITY OF WARWICK   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE;

ANIMAL; ARTICLE; CHEMISTRY; METABOLISM; PROTEIN QUATERNARY STRUCTURE;

ANIMALS; MOLECULAR CHAPERONES; PROTEIN STRUCTURE, QUATERNARY;

EID: 52449087558     PISSN: 15282511     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Conference Paper

References (34)

1. Anfinsen CB 1973 Principles that govern the folding of protein chains. Science 181:223-230
2. Barraclough BR, Ellis RJ 1980 Protein synthesis in chloroplasts. IX. Assembly of newly synthesized large subunits of ribulose bisphosphate carboxylase in isolated intact chloroplasts. Biochim Biophys Acta 608:19-31
3. Braig K, Otwinowski Z, Hegde R et al 1994 The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature 371:578-586
4. Buchberger A, Schroder H, Hesterkamp T, Schonfeld HJ, Bukau B 1996 Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding. J Mol Biol. 261:328-333
5. Deuerling E, Schulze-Specking A, Tomoyasu A, Mogk A, Bukau B 1999 Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature 400:693-696
6. Ellis RJ 1987 Proteins as molecular chaperones. Nature 328:378-379
7. Ellis RJ 1997 Do molecular chaperones have to be proteins? Biophys Res Commun 238:687-692
8. Ellis RJ 2001 Macromolecular crowding; obvious but underappreciated. Trends Biochem Sci 26:597-603
9. Ellis RJ 2003 Protein folding: the importance of the Anfinsen cage. Curr Biol 13:R881-883
10. Ellis RJ 2006 Molecular chaperones: assisting assembly in addition to folding. Trends Biochem Sci 31:395-401
11. Ellis RJ, Hemmingsen SM 1989 Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures. Trends Biochem Sci 14:339-342
12. Ellis RJ, Minton AP 2006 Protein aggregation in crowded environments. Biol Chem 387:485-497
13. Farr GW, Fenton WA, Rospert S, Horwich AR 2001 Folding with and without encapsulation by cis and trans-only GroEL-GroES complexes. EMBO J 22:3220-3230
14. Fayet O, Ziegelhoffer T, Georgopoulos C 1989 The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J Bacteriol 171:1379-1385
15. Goloubinoff P, Mogk A, Zvi AP, Tomoyasu T, Bukau B 1999 Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc Natl Acad Sci USA. 96:13732-13737
16. Hartl FU, Hayer-Hartl M 2002 Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295:1852-1858
17. Hemmingsen SM, Woolford C, van der Vies SM et al 1988 Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature 333:330-334
18. Horwich AL, Farr GW, Fenton WA 2006 GroEL-GroES-mediated protein folding. Chem Rev 106:1917-1930
19. Houry WA, Frishman D, Eckerskorn C, Lottspeich F, Hartl FU 1999 Identification of in vivo substrates of the chaperonin GroEL. Nature 402:147-154
20. Kaiser CM, Chang H-C, Agashe VR et al 2006 Real-time observation of trigger factor function on translating ribosomes. Nature 444:455-460
21. Kapatai G, Large A, Benesch JL et al 2006 All three chaperonin genes in the archaeon Haloferax volcanii are individually dispensable. Mol Microbiol 61:1583-1597
22. Kota J, Ljungdahl PO 2005 Specialized membrane-localized chaperones prevent aggregation of polytopic proteins in the ER. J Cell Biol 168:79-88
23. Kusukawa N, Yura T 1988 Heat shock protein GroE of Escherichia coli: key protective roles against thermal stress. Genes Dev 2:874-882
24. Laskey RA, Honda BM, Finch JT 1978 Nucleosomes are assembled by an acidic protein that binds histones and transfer them to DNA. Nature 275:416-420
25. Lund PA 2001 Molecular chaperones in the cell. Oxford University Press
26. Mogk A, Tomoyasu T, Goloubinoff P et al 1999 Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J 18:6934-6949
27. Nielsen KL, McLennan N, Masters M, Cowan NJ 1999 A single-ring mitochondrial chaperonin (HSP60-HSP10) can substitute for GroEL-GroES in vivo. J Bacteriol 181:5871-5875
28. Normington K, Kohno K, Kozutsumi Y, Gething MJ, Sambrook J 1989 S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell 57:1223-1236
29. Ostermann J, Horwich AL, Neupert W, Hartl F-U 1989 Protein folding in mitochondria requires complex formation with HSP60 and ATP hydrolysis. Nature 341:125-130
30. Smith DF 2001 Chaperones in signal transduction. In: Lund PA (ed) Molecular chaperones in the cell. Oxford University Press, p 164-179
31. Song J, Morimoto RI 2001 HSP70 chaperone networks. In: Lund PA (ed) Molecular chaperones in the cell. Oxford University Press, p 142-164
32. Ungewickell E 1985 The 70-kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles. EMBO J 4:3385-3391
33. Ursic D, Culbertson MR 1991 The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11:2629-2640
34. Young JC, Agashe VR, Siegers K, Hartl FU 2004 Pathways of chaperone-mediated protein folding in the cytosol. Nat Rev Cell Biol 5:781-790