Chaperone substrates inside the cell

Trends in Biochemical Sciences

Volumn 25, Issue 5, 2000, Pages 210-212

  Ellis, R John ^a  

^a UNIVERSITY OF WARWICK   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN;

CELL AGGREGATION; ESCHERICHIA COLI; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; REVIEW; STRESS;

ESCHERICHIA COLI;

EID: 0034194396     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(00)01576-0     Document Type: Short Survey

References (18)

1. Houry W.A.et al. Identification of in vivo substrates of the chaperonin GroEL. Nature. 402:1999;147-154.
2. Mogk A.et al. Identification of thermolabile E. coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 18:1999;6934-6949.
3. Sauer F.G.et al. PapD-like chaperones and pilus biogenesis. Semin. Cell Develop. Biol. 11:2000;27-34.
4. van den Berg B.et al. Effects of macromolecular crowding on protein folding and aggregation. EMBO J. 18:1999;6927-6933.
5. Sakikawa C.et al. On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES. J. Biol. Chem. 274:1999;21251-21256.
6. Ellis R.J., Hartl F.U. Principles of protein folding in the cellular environment. Curr. Opin. Struct. Biol. 9:1999;102-110.
7. Bukau B., Horwich A.L. The hsp70 and hsp60 chaperone machines. Cell. 92:1998;351-366.
8. Agashe V.R., Hartl F.U. Roles of molecular chaperones in cytoplasmic protein folding. Semin. Cell Develop. Biol. 11:2000;15-26.
9. Coyle J.E.et al. GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism. Fold. Design. 2:1997;R93-R104.
10. Bremer H., Dennis P.D. Modulation of chemical composition and other parameters of the cell by growth rate. Neidhardt F.C. Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology (Vol. 2). 1987;1527-1542 American Society for Microbiology, Washington, USA.
11. Netzer W.J., Hartl F.U. Protein folding in the cytosol: chaperonin-dependent and independent mechanisms. Trends Biochem. Sci. 23:1998;68-73.
12. Ewalt K.L.et al. In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell. 90:1997;491-500.
13. Deuerling E.et al. Trigger factor and DnaK cooperate in the folding of newly synthesized proteins. Nature. 400:1999;693-696.
14. Teter S.A.et al. Polypeptide flux through bacterial hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. Cell. 97:1999;755-765.
15. Goloubinoff P.et al. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl. Acad. Sci. U. S. A. 96:1999;13732-13737.
16. Glover J.R., Lindquist S. Hsp104, hsp70 and hsp40; a novel chaperone system that rescues previously aggregated proteins. Cell. 94:1998;73-82.
17. Garel J.-R. Large multidomain and multisubunit proteins. Creighton T.E. Protein Folding. 1992;405-454 W.H. Freeman.
18. Schlunegger M.P.et al. Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. Adv. Protein Chem. 50:1997;61-122.