| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
Protein Science, Vol 1, Issue 3 363-369, Copyright © 1992 by Cold Spring Harbor Laboratory Press
ARTICLE |
P. V. VIITANEN, A. A. GATENBY and G. H. LORIMER
Central Research and Development Department, E.I. Du Pont de Nemours & Co. Experimental Station, Wilmington, Delaware 19880-0402
In vitro experiments exploying the soluble proteins from Escherichia coli reveal that about half of them, in their unfolded or partially folded states, but not in their native states, can form stable binary complexes with chaperonin 60 (groEL). These complexes can be isolated by gel filtration chromatography and are efficiently discharged upon the addition of Mg.ATP. Binary complex formation is substantially reduced if chaperonin 60 is presaturated with Rubisco-I, the folding intermediate of Rubisco, but not with native Rubisco. Binary complex formation is also reduced if the transient species that interact with chaperonin 60 are permitted to progress to more stable states. This implies that the structural elements or motifs that are recognized by chaperonin 60 and that are responsible for binary complex formation are only present or accessible in the unfolded states of proteins or in certain intermediates along their respective folding pathways. Given the high-affinity binding that we have observed in the present study and the normal cellular abundance of chaperonin 60, we suspect that the folding of most proteins in E. coli does not occur in free solution spontaneously, but instead takes place while they are associated with molecular chaperones.
CiteULike 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  T. Nojima, S. Murayama, M. Yoshida, and F. Motojima Determination of the Number of Active GroES Subunits in the Fused Heptamer GroES Required for Interactions with GroEL J. Biol. Chem., June 27, 2008; 283(26): 18385 - 18392. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 O. Noivirt-Brik, R. Unger, and A. Horovitz Low folding propensity and high translation efficiency distinguish in vivo substrates of GroEL from other Escherichia coli proteins Bioinformatics, December 15, 2007; 23(24): 3276 - 3279. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Paul, C. Singh, S. Mishra, and T. K. Chaudhuri The 69 kDa Escherichia coli maltodextrin glucosidase does not get encapsulated underneath GroES and folds through trans mechanism during GroEL/GroES-assisted folding FASEB J, September 1, 2007; 21(11): 2874 - 2885. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 G. Stan, G. H. Lorimer, D. Thirumalai, and B. R. Brooks Coupling between allosteric transitions in GroEL and assisted folding of a substrate protein PNAS, May 22, 2007; 104(21): 8803 - 8808. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. W. Farr, W. A. Fenton, and A. L. Horwich Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL PNAS, March 27, 2007; 104(13): 5342 - 5347. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Stan, B. R. Brooks, G. H. Lorimer, and D. Thirumalai Residues in substrate proteins that interact with GroEL in the capture process are buried in the native state PNAS, March 21, 2006; 103(12): 4433 - 4438. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 O. V. Polyakova, O. Roitel, R. A. Asryants, A. A. Poliakov, G. Branlant, and V. I. Muronetz Misfolded forms of glyceraldehyde-3-phosphate dehydrogenase interact with GroEL and inhibit chaperonin-assisted folding of the wild-type enzyme Protein Sci., April 1, 2005; 14(4): 921 - 928. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Stan, B. R. Brooks, G. H. Lorimer, and D. Thirumalai Identifying natural substrates for chaperonins using a sequence-based approach Protein Sci., January 1, 2005; 14(1): 193 - 201. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. Ogino, M. Wachi, A. Ishii, N. Iwai, T. Nishida, S. Yamada, K. Nagai, and M. Sugai FtsZ-dependent localization of GroEL protein at possible division sites Genes Cells, September 1, 2004; 9(9): 765 - 771. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. Kuchanny-Ardigo and B. Lipinska Cloning and characterization of the groE heat-shock operon of the marine bacterium Vibrio harveyi Microbiology, June 1, 2003; 149(6): 1483 - 1492. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. Aoki, F. Motojima, H. Taguchi, T. Yomo, and M. Yoshida GroEL Binds Artificial Proteins with Random Sequences J. Biol. Chem., April 28, 2000; 275(18): 13755 - 13758. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. Dickson, C. Weiss, R. J. Howard, S. P. Alldrick, R. J. Ellis, G. Lorimer, A. Azem, and P. V. Viitanen Reconstitution of Higher Plant Chloroplast Chaperonin 60 Tetradecamers Active in Protein Folding J. Biol. Chem., April 14, 2000; 275(16): 11829 - 11835. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
O. Kandror, M. Sherman, and A. Goldberg Rapid Degradation of an Abnormal Protein in Escherichia coli Proceeds through Repeated Cycles of Association with GroEL J. Biol. Chem., December 31, 1999; 274(53): 37743 - 37749. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. Belles, A. Kuhl, R. Nosheny, and S. R. Carding Plasma Membrane Expression of Heat Shock Protein 60 In Vivo in Response to Infection Infect. Immun., August 1, 1999; 67(8): 4191 - 4200. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. Sakikawa, H. Taguchi, Y. Makino, and M. Yoshida On the Maximum Size of Proteins to Stay and Fold in the Cavity of GroEL underneath GroES J. Biol. Chem., July 23, 1999; 274(30): 21251 - 21256. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. D. Andreadis and L. W. Black Substrate Mutations That Bypass a Specific Cpn10 Chaperonin Requirement for Protein Folding J. Biol. Chem., December 18, 1998; 273(51): 34075 - 34086. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
P. A. Voziyan, B. C. Tieman, C.-M. Low, and M. T. Fisher Changing the Nature of the Initial Chaperonin Capture Complex Influences the Substrate Folding Efficiency J. Biol. Chem., September 25, 1998; 273(39): 25073 - 25078. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. Torella, J. R. Mattingly Jr., A. Artigues, A. Iriarte, and M. Martinez-Carrion Insight into the Conformation of Protein Folding Intermediate(s) Trapped by GroEL J. Biol. Chem., February 13, 1998; 273(7): 3915 - 3925. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
B. T. Brazil, J. Ybarra, and P. M. Horowitz Divalent Cations Can Induce the Exposure of GroEL Hydrophobic Surfaces and Strengthen GroEL Hydrophobic Binding Interactions. NOVEL EFFECTS OF Zn2+ GroEL INTERACTIONS J. Biol. Chem., February 6, 1998; 273(6): 3257 - 3263. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. E. Churchich Conformational Changes at the Nucleotide Binding of GroEL Induced by Binding of Protein Substrates. LUMINESCENCE STUDIES J. Biol. Chem., August 8, 1997; 272(32): 19645 - 19648. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
B. M. Gorovits, J. Ybarra, and P. M. Horowitz ATP Hydrolysis Is Critical for Induction of Conformational Changes in GroEL That Expose Hydrophobic Surfaces J. Biol. Chem., March 14, 1997; 272(11): 6842 - 6845. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. Zahn, A. M. Buckle, S. Perrett, C. M. Johnson, F. J. Corrales, R. Golbik, and A. R. Fersht Chaperone activity and structure of monomeric polypeptide binding domains of GroEL PNAS, December 24, 1996; 93(26): 15024 - 15029. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. d. Crouy-Chanel, M. Kohiyama, and G. Richarme Specificity of DnaK for Arginine/Lysine and Effect of DnaJ on the Amino Acid Specificity of DnaK J. Biol. Chem., June 28, 1996; 271(26): 15486 - 15490. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. L. Gibbons and P. M. Horowitz Ligand-induced Conformational Changes in the Apical Domain of the Chaperonin GroEL J. Biol. Chem., January 5, 1996; 271(1): 238 - 243. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Tian, I. E. Vainberg, W. D. Tap, S. A. Lewis, and N. J. Cowan Quasi-native Chaperonin-bound Intermediates in Facilitated Protein Folding J. Biol. Chem., October 13, 1995; 270(41): 23910 - 23913. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Ybarra and P. M. Horowitz Inactive GroEL Monomers Can Be Isolated and Reassembled to Functional Tetradecamers That Contain Few Bound Peptides J. Biol. Chem., September 29, 1995; 270(39): 22962 - 22967. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Ybarra and P. M. Horowitz Refolding and Reassembly of Active Chaperonin GroEL After Denaturation J. Biol. Chem., September 22, 1995; 270(38): 22113 - 22115. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. E. Smith and M. T. Fisher Interactions between the GroE Chaperonins and Rhodanese J. Biol. Chem., September 15, 1995; 270(37): 21517 - 21523. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
P. V. Viitanen, M. Schmidt, J. Buchner, T. Suzuki, E. Vierling, R. Dickson, G. H. Lorimer, A. Gatenby, and J. Soll Functional Characterization of the Higher Plant Chloroplast Chaperonins J. Biol. Chem., July 28, 1995; 270(30): 18158 - 18164. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
B. M. Gorovits and P. M. Horowitz The Molecular Chaperonin cpn60 Displays Local Flexibility That Is Reduced after Binding with an Unfolded Protein J. Biol. Chem., June 2, 1995; 270(22): 13057 - 13062. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. L. Gibbons and D. L. Gibbons Exposure of Hydrophobic Surfaces on the Chaperonin GroEL Oligomer by Protonation or Modification of His-401 J. Biol. Chem., March 31, 1995; 270(13): 7335 - 7340. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
P. M. Horowitz, S. Hua, and D. L. Gibbons Hydrophobic Surfaces That Are Hidden in Chaperonin Cpn60 Can Be Exposed by Formation of Assembly-Competent Monomers or by Ionic Perturbation of the Oligomer J. Biol. Chem., January 27, 1995; 270(4): 1535 - 1542. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Z. Lin, F. P. Schwarz, and E. Eisenstein The Hydrophobic Nature of GroEL-Substrate Binding J. Biol. Chem., January 20, 1995; 270(3): 1011 - 1014. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A.L. Horwich, J.S. Weissman, and W.A. Fenton Kinesis of Polypeptide during GroEL-mediated Folding Cold Spring Harb Symp Quant Biol, January 1, 1995; 60(0): 435 - 440. [Abstract] [PDF]
|
|
|
|
 |
|
 A Azem, M Kessel, and P Goloubinoff Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer Science, July 29, 1994; 265(5172): 653 - 656. [Abstract] [PDF]
|
|
|
|
|
|
M Schmidt, K Rutkat, R Rachel, G Pfeifer, R Jaenicke, P Viitanen, G Lorimer, and J Buchner Symmetric complexes of GroE chaperonins as part of the functional cycle Science, July 29, 1994; 265(5172): 656 - 659. [Abstract] [PDF]
|
|
|
|
|
|
M. Todd, P. Viitanen, and G. Lorimer Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding Science, July 29, 1994; 265(5172): 659 - 666. [Abstract] [PDF]
|
|
|
|
|
|
B. C. Tieman, M. F. Johnston, and M. T. Fisher A Comparison of the GroE Chaperonin Requirements for Sequentially and Structurally Homologous Malate Dehydrogenases. THE IMPORTANCE OF FOLDING KINETICS AND SOLUTION ENVIRONMENT J. Biol. Chem., November 21, 2001; 276(48): 44541 - 44550. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
