Coiled coils meet the chaperone world

Trends in Biochemical Sciences

Volumn 29, Issue 9, 2004, Pages 455-458

  Martin, Jörg ^a   Gruber, Markus ^a   Lupas, Andrei N ^a  

^a MAX PLANCK INSTITUTE FOR DEVELOPMENTAL BIOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE;

ENZYME BINDING; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; SHORT SURVEY;

ADENOSINE TRIPHOSPHATASES; ARCHAEAL PROTEINS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; PROTEIN CONFORMATION; PROTEIN SUBUNITS; SUBSTRATE SPECIFICITY;

EID: 4344679972     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2004.07.004     Document Type: Short Survey

References (18)

1. A. Lupas Coiled coils: new structures and new functions Trends Biochem. Sci. 21 1996 375 382
2. F.U. Hartl, and M. Hayer-Hartl Molecular chaperones in the cytosol: from nascent chain to folded protein Science 295 2002 1852 1858
3. S. Geissler A novel protein complex promoting formation of functional α- and γ-tubulin EMBO J. 17 1998 952 966
4. I.E. Vainberg Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin Cell 93 1998 863 873
5. K. Siegers Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system EMBO J. 18 1999 75 84
6. M.R. Leroux MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin EMBO J. 18 1999 6730 6743
7. R. Siegert Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins Cell 103 2000 621 632
8. V.F. Lundin Molecular clamp mechanism of substrate binding by hydrophobic coiled-coil residues of the archaeal chaperone prefoldin Proc. Natl. Acad. Sci. U. S. A. 101 2004 4367 4372
9. C.T. Simons Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding J. Biol. Chem. 279 2004 4196 4203
10. O. Llorca Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi-native conformations EMBO J. 19 2000 5971 5979
11. O. Llorca The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin EMBO J. 20 2001 4065 4075
12. M.R. Leroux, and F.U. Hartl Protein folding: versatility of the cytosolic chaperonin TRiC/CCT Curr. Biol. 10 2000 R260 R264
13. S. Lee The ClpB/Hsp104 molecular chaperone - a protein disaggregating machine J. Struct. Biol. 146 2004 99 105
14. S. Lee The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state Cell 115 2003 229 240
15. M. Rohrwild HslV-HslU: a novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome Proc. Natl. Acad. Sci. U. S. A. 93 1996 5808 5813
16. H.K. Song Mutational studies on HslU and its docking mode with HslV Proc. Natl. Acad. Sci. U. S. A. 97 2000 14103 14108
17. M. Nitsch Group II chaperonin in an open conformation examined by electron tomography Nat. Struct. Biol. 5 1998 855 857
18. M.C. Sousa Crystal and solution structures of an HslUV protease-chaperone complex Cell 103 2000 633 643