Coiled coils meet the chaperone world.

Coiled coils are versatile structural modules that engage in a variety of cellular activities. Recent studies illuminate their role as substrate-binding elements in the chaperone cofactor prefoldin and in the AAA+ ATPases involved in protein (un)folding processes. The use of coiled coils to mediate the binding of non-native proteins represents a novel strategy in chaperone design and a new function for coiled coils.

[1]  M. Sowa,et al.  The ClpB/Hsp104 molecular chaperone-a protein disaggregating machine. , 2004, Journal of structural biology.

[2]  Wolfgang Baumeister,et al.  Group II chaperonin in an open conformation examined by electron tomography , 1998, Nature Structural Biology.

[3]  F. Hartl,et al.  Protein folding: Versatility of the cytosolic chaperonin TRiC/CCT , 2000, Current Biology.

[4]  J Martín-Benito,et al.  Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi‐native conformations , 2000, The EMBO journal.

[5]  Christine B. Trame,et al.  Crystal and Solution Structures of an HslUV Protease–Chaperone Complex , 2000, Cell.

[6]  F. Hartl,et al.  Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein , 2002, Science.

[7]  J. Mwenifumbo,et al.  Molecular clamp mechanism of substrate binding by hydrophobic coiled-coil residues of the archaeal chaperone prefoldin. , 2004, Proceedings of the National Academy of Sciences of the United States of America.

[8]  K. Willison,et al.  The ‘sequential allosteric ring’ mechanism in the eukaryotic chaperonin‐assisted folding of actin and tubulin , 2001, The EMBO journal.

[9]  C. Dobson,et al.  MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin , 1999, The EMBO journal.

[10]  Wah Chiu,et al.  The Structure of ClpB A Molecular Chaperone that Rescues Proteins from an Aggregated State , 2003, Cell.

[11]  A. Lupas Coiled coils: new structures and new functions. , 1996, Trends in biochemical sciences.

[12]  R. Huber,et al.  Mutational studies on HslU and its docking mode with HslV. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[13]  F. Hartl,et al.  Structure of the Molecular Chaperone Prefoldin Unique Interaction of Multiple Coiled Coil Tentacles with Unfolded Proteins , 2000, Cell.

[14]  J. Vandekerckhove,et al.  Prefoldin, a Chaperone that Delivers Unfolded Proteins to Cytosolic Chaperonin , 1998, Cell.

[15]  K. Siegers,et al.  A novel protein complex promoting formation of functional α‐ and γ‐tubulin , 1998, The EMBO journal.

[16]  A. Shevchenko,et al.  Compartmentation of protein folding in vivo: sequestration of non‐native polypeptide by the chaperonin–GimC system , 1999, The EMBO journal.

[17]  C. Ampe,et al.  Selective Contribution of Eukaryotic Prefoldin Subunits to Actin and Tubulin Binding* , 2004, Journal of Biological Chemistry.

[18]  A. Goldberg,et al.  HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome. , 1996, Proceedings of the National Academy of Sciences of the United States of America.