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Science 8 March 2002:
Vol. 295. no. 5561, pp. 1852 - 1858
DOI: 10.1126/science.1068408
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Review

Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein

F. Ulrich Hartl, Manajit Hayer-Hartl

Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones, which serve to prevent protein misfolding and aggregation in the crowded environment of the cell. Nascent chain-binding chaperones, including trigger factor, Hsp70, and prefoldin, stabilize elongating chains on ribosomes in a nonaggregated state. Folding in the cytosol is achieved either on controlled chain release from these factors or after transfer of newly synthesized proteins to downstream chaperones, such as the chaperonins. These are large, cylindrical complexes that provide a central compartment for a single protein chain to fold unimpaired by aggregation. Understanding how the thousands of different proteins synthesized in a cell use this chaperone machinery has profound implications for biotechnology and medicine.

Department of Cellular Biochemistry, Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, D-82152 Martinsried, Germany.
*To whom correspondence should be addressed. E-mail: uhartl{at}biochem.mpg.de

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Testing the Neutral Fixation of Hetero-Oligomerism in the Archaeal Chaperonin CCT.
V. Ruano-Rubio and M. A. Fares (2007)
Mol. Biol. Evol. 24, 1384-1396
   Abstract »    Full Text »    PDF »
Functional Interaction between Phosducin-like Protein 2 and Cytosolic Chaperonin Is Essential for Cytoskeletal Protein Function and Cell Cycle Progression.
P. C. Stirling, M. Srayko, K. S. Takhar, A. Pozniakovsky, A. A. Hyman, and M. R. Leroux (2007)
Mol. Biol. Cell 18, 2336-2345
   Abstract »    Full Text »    PDF »
The Mrj co-chaperone mediates keratin turnover and prevents the formation of toxic inclusion bodies in trophoblast cells of the placenta.
E. D. Watson, C. Geary-Joo, M. Hughes, and J. C. Cross (2007)
Development 134, 1809-1817
   Abstract »    Full Text »    PDF »
Network of general and specialty J protein chaperones of the yeast cytosol.
C. Sahi and E. A. Craig (2007)
PNAS 104, 7163-7168
   Abstract »    Full Text »    PDF »
Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL.
G. W. Farr, W. A. Fenton, and A. L. Horwich (2007)
PNAS 104, 5342-5347
   Abstract »    Full Text »    PDF »
Heat Shock Factor 2 (HSF2) Contributes to Inducible Expression of hsp Genes through Interplay with HSF1.
P. Ostling, J. K. Bjork, P. Roos-Mattjus, V. Mezger, and L. Sistonen (2007)
J. Biol. Chem. 282, 7077-7086
   Abstract »    Full Text »    PDF »


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