Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

Folding of two monomeric enzymes mediated by groE has been reconstituted in vitro. The groEL protein stabilizes the polypeptides in a conformation resembling the 'molten globule' state. Mg–ATP and groES then promote the acquisition of ordered tertiary structure at the surface of groEL. Folding requires the hydrolysis of about 100 ATP molecules per protein monomer. This active process of surface-mediated chain folding might represent a general mechanism for the formation of protein structure in vivo.

[1]  N. Sternberg.  Properties of a mutant of Escherichia coli defective in bacteriophage λ head formation (groE) , 1973 .

[2]  N. Lissin,et al.  Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein , 1988, Nature.

[3]  F. Hartl,et al.  Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis , 1989, Nature.

[4]  D. Vestweber,et al.  A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein. , 1990, The EMBO journal.

[5]  R. Ellis,et al.  Dissociation of the ribulosebisphosphate-carboxylase large-subunit binding protein into dissimilar subunits. , 1987, European journal of biochemistry.

[6]  Elizabeth A. Craig,et al.  Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins , 1990, Nature.

[7]  A. Engel,et al.  Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly. , 1979, Journal of molecular biology.

[8]  C. Georgopoulos,et al.  Purification and properties of the groES morphogenetic protein of Escherichia coli. , 1986, The Journal of biological chemistry.

[9]  R. Larossa,et al.  Demonstration by genetic suppression of interaction of GroE products with many proteins , 1989, Nature.

[10]  P. Horowitz,et al.  Reversible folding of rhodanese. Presence of intermediate(s) at equilibrium. , 1989, The Journal of biological chemistry.

[11]  S. Lehrer.  Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. , 1971, Biochemistry.

[12]  T. Creighton,et al.  The molten globule protein conformation probed by disulphide bonds , 1991, Nature.

[13]  K. Kuwajima,et al.  The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structure , 1989, Proteins.

[14]  G. Lorimer,et al.  Identification of a groES-like chaperonin in mitochondria that facilitates protein folding. , 1990, Proceedings of the National Academy of Sciences of the United States of America.

[15]  P. Horowitz,et al.  The detection of kinetic intermediate(s) during refolding of rhodanese. , 1990, The Journal of biological chemistry.

[16]  P. Horowitz,et al.  Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effect of lauryl maltoside. , 1986, The Journal of biological chemistry.

[17]  A. Horwich,et al.  The mitochondrial chaperonin hsp60 is required for its own assembly. , 1990 .

[18]  B. Kaufman,et al.  Primary structure of chicken liver dihydrofolate reductase. , 1980, Biochemistry.

[19]  A. D. Kaiser,et al.  Host participation in bacteriophage lambda head assembly. , 1973, Journal of molecular biology.

[20]  A. Goldberg,et al.  Selectivity of intracellular proteolysis: protein substrates activate the ATP-dependent protease (La). , 1986, Science.

[21]  G. Lorimer,et al.  Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP , 1989, Nature.

[22]  O. Ptitsyn,et al.  Sequential mechanism of refolding of carbonic anhydrase B , 1987, FEBS letters.

[23]  R. Jaenicke,et al.  Folding and association of proteins. , 1982, Biophysics of structure and mechanism.

[24]  R. Ellis,et al.  Protein synthesis in chloroplasts. IX. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated intact pea chloroplasts. , 1980, Biochimica et biophysica acta.

[25]  A. Vachereau.  Luminescent immunodetection of western-blotted proteins from coomassie-stained polyacrylamide gel. , 1989, Analytical biochemistry.

[26]  Ellis Rj,et al.  Chaperone Function: The Assembly of Ribulose Bisphosphate Carboxylase-Oxygenase , 1990 .

[27]  W. Hol,et al.  The covalent and tertiary structure of bovine liver rhodanese , 1978, Nature.

[28]  R. Jaenicke,et al.  GroE facilitates refolding of citrate synthase by suppressing aggregation. , 1991, Biochemistry.

[29]  R. Pérez-Montfort,et al.  Causes of the decrease in fluorescence due to proteolysis of α-casein , 1990 .

[30]  C. Georgopoulos,et al.  Three pure chaperone proteins of Escherichia coli‐‐SecB, trigger factor and GroEL‐‐form soluble complexes with precursor proteins in vitro. , 1989, The EMBO journal.

[31]  A. Myers,et al.  Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor , 1989, Nature.

[32]  R. Freedman.  Protein disulfide isomerase: Multiple roles in the modification of nascent secretory proteins , 1989, Cell.

[33]  O. Ptitsyn,et al.  Evidence for a molten globule state as a general intermediate in protein folding , 1990, FEBS letters.

[34]  R. Hallberg,et al.  A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene , 1988, Molecular and Cellular Biology.

[35]  F. Schmid,et al.  The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell. , 1990, Biochemistry.

[36]  A. Plückthun,et al.  The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta‐lactamase precursor. , 1990, The EMBO journal.

[37]  J M Burridge,et al.  Refined crystal structures of Escherichia coli and chicken liver dihydrofolate reductase containing bound trimethoprim. , 1985, The Journal of biological chemistry.

[38]  Roger W. Hendrix,et al.  Homologous plant and bacterial proteins chaperone oligomeric protein assembly , 1988, Nature.

[39]  J. Rothman.  Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells , 1989, Cell.

[40]  A hydrophobic cluster forms early in the folding of dihydrofolate reductase , 1989, Proteins.

[41]  Hugh Pelham,et al.  Coming in from the cold , 2006, Nature.

[42]  F. Hartl,et al.  Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria , 1989, Nature.

[43]  X. Tan,et al.  Effects of conversion of an invariant tryptophan residue to phenylalanine on the function of human dihydrofolate reductase. , 1989, Biochemistry.

[44]  R. Hendrix.  Purification and properties of groE, a host protein involved in bacteriophage assembly. , 1979, Journal of molecular biology.

[45]  G. Lorimer,et al.  Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent. , 1990, Biochemistry.

[46]  J. Rothman,et al.  Peptide binding and release by proteins implicated as catalysts of protein assembly. , 1989, Science.

[47]  W. Wickner,et al.  The ATPase activity of secA is regulated by acidic phospholipids, secY, and the leader and mature domains of precursor proteins , 1990, Cell.

[48]  Matthews Cr,et al.  Folding of dihydrofolate reductase from Escherichia coli , 1986 .

[49]  J. Ellis.  Proteins as molecular chaperones , 1987, Nature.