groes protein

Summary

Summary: A chaperonin 10 heat-shock protein isolated from Escherichia coli.

Top Publications

  1. ncbi Machinery of protein folding and unfolding
    Xiaodong Zhang
    Centre for Structural Biology, Department of Biological Sciences, Imperial College of Science, Technology and Medicine, Flowers Building, South Kensington, SW7 2AZ, London, UK
    Curr Opin Struct Biol 12:231-8. 2002
  2. pmc Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones
    Ario de Marco
    Protein Expression Unit, European Molecular Biology Laboratory, Heidelberg, Germany
    Cell Stress Chaperones 10:329-39. 2005
  3. pmc Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics
    Charu Chaudhry
    Department of Molecular Biophysics and Biochemistry and Howard Hughes Medical Institute, Yale University, New Haven, CT, USA
    EMBO J 22:4877-87. 2003
  4. ncbi Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein
    Yun Chi Tang
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Cell 125:903-14. 2006
  5. ncbi Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli
    Michael J Kerner
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Cell 122:209-20. 2005
  6. ncbi Directed evolution of substrate-optimized GroEL/S chaperonins
    Jue D Wang
    Howard Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California, San Francisco 94143, USA
    Cell 111:1027-39. 2002
  7. ncbi The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    Z Xu
    The Howard Hughes Medical Institute, The Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510, USA
    Nature 388:741-50. 1997
  8. ncbi A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation
    B Trevor Sewell
    Electron Microscope Unit and Department of Chemistry, University of Cape Town, Rondebosch, South Africa
    Nat Struct Mol Biol 11:1128-33. 2004
  9. ncbi Molecular mechanisms of chaperonin GroEL-GroES function
    O Keskin
    Molecular Structure Section, Laboratory of Experimental and Computational Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
    Biochemistry 41:491-501. 2002
  10. ncbi Residues in chaperonin GroEL required for polypeptide binding and release
    W A Fenton
    Department of Genetics, Yale University School of Medicine, Boyer Center, New Haven, Connecticut 06510
    Nature 371:614-9. 1994

Scientific Experts

Detail Information

Publications154 found, 100 shown here

  1. ncbi Machinery of protein folding and unfolding
    Xiaodong Zhang
    Centre for Structural Biology, Department of Biological Sciences, Imperial College of Science, Technology and Medicine, Flowers Building, South Kensington, SW7 2AZ, London, UK
    Curr Opin Struct Biol 12:231-8. 2002
    ..The majority of folding/unfolding machines adopt oligomeric ring structures in a cooperative fashion and utilise the conformational changes induced by ATP binding/hydrolysis for their specific functions...
  2. pmc Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones
    Ario de Marco
    Protein Expression Unit, European Molecular Biology Laboratory, Heidelberg, Germany
    Cell Stress Chaperones 10:329-39. 2005
    ....
  3. pmc Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics
    Charu Chaudhry
    Department of Molecular Biophysics and Biochemistry and Howard Hughes Medical Institute, Yale University, New Haven, CT, USA
    EMBO J 22:4877-87. 2003
    ..We discuss the likely basis of the ability of gamma-phosphate binding to convert preformed GroEL-GroES-ADP-polypeptide complexes into the folding-active state...
  4. ncbi Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein
    Yun Chi Tang
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Cell 125:903-14. 2006
    ..We suggest that by combining these features, the chaperonin cage provides a physical environment optimized to catalyze the structural annealing of proteins with kinetically complex folding pathways...
  5. ncbi Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli
    Michael J Kerner
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Cell 122:209-20. 2005
    ..We suggest that the chaperonin system may have facilitated the evolution of this fold into a versatile platform for the implementation of numerous enzymatic functions...
  6. ncbi Directed evolution of substrate-optimized GroEL/S chaperonins
    Jue D Wang
    Howard Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California, San Francisco 94143, USA
    Cell 111:1027-39. 2002
    ..This conflict and the nature of the ring structure may help explain the evolution of cellular chaperone systems...
  7. ncbi The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    Z Xu
    The Howard Hughes Medical Institute, The Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510, USA
    Nature 388:741-50. 1997
    ..When combined with new functional results, this negative allosteric mechanism suggests a model for an ATP-driven folding cycle that requires a double toroid...
  8. ncbi A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation
    B Trevor Sewell
    Electron Microscope Unit and Department of Chemistry, University of Cape Town, Rondebosch, South Africa
    Nat Struct Mol Biol 11:1128-33. 2004
    ..Lacking the allosteric signal from the opposite ring, these complexes cannot release their GroES and become trapped, dead-end states...
  9. ncbi Molecular mechanisms of chaperonin GroEL-GroES function
    O Keskin
    Molecular Structure Section, Laboratory of Experimental and Computational Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
    Biochemistry 41:491-501. 2002
    ..These modes of motion could be used to manipulate the substrate's conformations...
  10. ncbi Residues in chaperonin GroEL required for polypeptide binding and release
    W A Fenton
    Department of Genetics, Yale University School of Medicine, Boyer Center, New Haven, Connecticut 06510
    Nature 371:614-9. 1994
    ..A highly conserved residue, Asp 87, positioned within a putative nucleotide-binding pocket in the top of the equatorial domain, is essential for ATP hydrolysis and polypeptide release...
  11. pmc A mobile loop order-disorder transition modulates the speed of chaperonin cycling
    Frank Shewmaker
    Department of Biochemistry, Tulane University Health Sciences Center, New Orleans, Louisiana 70112, USA
    Protein Sci 13:2139-48. 2004
    ..Thus, the free energy of mobile-loop ordering and disordering acts like the inertia of an engine's flywheel by modulating the speed of chaperonin conformational changes...
  12. ncbi Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations
    Itamar Kass
    Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel
    Proteins 48:611-7. 2002
    ..The results are discussed in the context of available structural, genetic, and biochemical data concerning short- and long-range interactions in the GroE system...
  13. ncbi Chaperonin-mediated protein folding: fate of substrate polypeptide
    Wayne A Fenton
    Department of Genetics, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06510, USA
    Q Rev Biophys 36:229-56. 2003
    ....
  14. pmc Translocation boost protein-folding efficiency of double-barreled chaperonins
    Ivan Coluzza
    Cambridge University Centre for Computational Chemistry, Department of Chemistry, Cambridge, United Kingdom
    Biophys J 90:3375-81. 2006
    ..Moreover, we argue that internal folding is both more efficient and safer than a scenario where partially refolded proteins escape from the complex before being recaptured...
  15. ncbi The disordered mobile loop of GroES folds into a defined beta-hairpin upon binding GroEL
    F Shewmaker
    Department of Biochemistry, Tulane University Health Sciences Center, New Orleans, Louisiana 70112-2699, USA
    J Biol Chem 276:31257-64. 2001
    ..Analysis of sequence conservation suggests that sequences of the mobile loop and strongly binding peptide were selected for the ability to adopt this hairpin conformation...
  16. pmc Bacteriophage-encoded cochaperonins can substitute for Escherichia coli's essential GroES protein
    France Keppel
    Departement de Biochimie Medicale, Centre Medicale Universitaire, Geneva, Switzerland
    EMBO Rep 3:893-8. 2002
    ..Thus, it appears that, despite very little sequence identity with groES, the bacteriophage-encoded Gp31 and CocO proteins are capable of replacing GroES in the folding of E. coli's essential, housekeeping proteins...
  17. ncbi The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coli
    A Richardson
    Departement de Biochimie Medicale, Centre Medical Universitaire, 1 rue Michel Servet, 1211 Geneva, Switzerland
    J Biol Chem 276:4981-7. 2001
    ..It seems likely that the single ring mitochondrial Hsp60 exhibits intrinsically lower affinity for the co-chaperonin that can be compensated for by a higher affinity mobile loop...
  18. ncbi Isolation and analysis of mutant alleles of the Bacillus subtilis HrcA repressor with reduced dependency on GroE function
    Silke Reischl
    Institute of Genetics, University of Bayreuth, Universitaetsstrasse 30, Bayreuth D 95440, Germany
    J Biol Chem 277:32659-67. 2002
    ..All these experimental data are in full agreement with our previously published model that HrcA needs the GroE chaperonin system for activation...
  19. ncbi An expanded protein folding cage in the GroEL-gp31 complex
    Daniel K Clare
    School of Crystallography, Birkbeck College, University of London, Malet Street, London WC1E 7HX, UK
    J Mol Biol 358:905-11. 2006
    ..At 56 kDa, gp23 is close to the maximum size limit of a polypeptide that is thought to fit inside the GroEL-GroES folding cage...
  20. ncbi Assembly of chaperonin complexes
    A R Kusmierczyk
    Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Box G-J2, Providence, RI 02912, USA
    Mol Biotechnol 19:141-52. 2001
    ..Interestingly, the intracellular assembly of type I chaperonins appears to be a chaperone-dependent process itself and requires functional preformed chaperonin complexes...
  21. ncbi Purification and characterization of the GroESLx chaperonins from the symbiotic X-bacteria in Amoeba proteus
    G H Jung
    School of Biological Sciences, Seoul, 151-742, Korea
    Protein Expr Purif 23:459-67. 2001
    ..In this study, we developed a method for the purification of GroESLx and demonstrated that their chaperonin function is homologous to GroESL of E. coli...
  22. ncbi Chaperonin-mediated de novo generation of prion protein aggregates
    J Stockel
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, D 82152, Germany
    J Mol Biol 313:861-72. 2001
    ..These results show that chaperonins of the Hsp60 class can, in principle, mediate PrP aggregation de novo, i.e. independently of a pre-existent PrP(Sc) template...
  23. ncbi The ins and outs of GroEL-mediated protein folding
    J S Weissman
    Howard Hughes Medical Institute, Department of Cellular and Molecular Pharmacology, University of California-San Francisco, San Francisco, CA 94143, USA
    Mol Cell 8:730-2. 2001
    ..The second defines a confinement-independent pathway, which allows GroEL to assist folding of substrates too large to be encapsulated...
  24. ncbi GroEL/GroES-mediated folding of a protein too large to be encapsulated
    T K Chaudhuri
    Howard Hughes Medical Institute, Department of Genetics, Yale University School of Medicine, Boyer Center, New Haven, CT 06510, USA
    Cell 107:235-46. 2001
    ..Following the phase of ATP/GroES-dependent refolding, GroEL stably bound apoaconitase, releasing active holoenzyme upon Fe(4)S(4) cofactor formation, independent of ATP and GroES...
  25. ncbi Dual function of protein confinement in chaperonin-assisted protein folding
    A Brinker
    Department of Cellular Biochemistry, Max-Planck-Institute of Biochemistry, 82152 Martinsried, Germany
    Cell 107:223-33. 2001
    ....
  26. pmc Factors governing the substrate recognition by GroEL chaperone: a sequence correlation approach
    Tapan K Chaudhuri
    Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology Delhi, Hauz Khas, New Delhi 110016, India
    Cell Stress Chaperones 10:24-36. 2005
    ....
  27. ncbi Expression, purification, and characterization of a novel recombinant fusion protein, rhTPO/SCF, in Escherichia coli
    Yuhui Zang
    State Key Laboratory of Pharmaceutical Biotechnology, School of Life Science, Nanjing University, PR China
    Protein Expr Purif 47:427-33. 2006
    ..Western blot analysis confirmed the identity of the purified protein. rhTPO/SCF stimulated a dose-dependent cell proliferation in both TF1 and Mo7e cell lines...
  28. ncbi Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states
    Charu Chaudhry
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA
    J Mol Biol 342:229-45. 2004
    ....
  29. ncbi Mechanisms of ATPases--a multi-disciplinary approach
    Mathieu Rappas
    Centre for Structural Biology, Department of Biological Sciences, Imperial College London, Flowers Building, South Kensington London SW7 2AZ, UK
    Curr Protein Pept Sci 5:89-105. 2004
    ..We will therefore discuss them in greater details in order to describe the wide range techniques being utilised...
  30. ncbi DnaK and DnaJ facilitated the folding process and reduced inclusion body formation of magnesium transporter CorA overexpressed in Escherichia coli
    Yong Chen
    Skirball Institute of Biomolecular Medicine and Department of Cell Biology, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA
    Protein Expr Purif 32:221-31. 2003
    ..These co-expression systems can be used for producing other membrane proteins in large quantities...
  31. ncbi Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK
    S Vorderwülbecke
    Ciphergen Biosystems GmbH, Hannah Vogt Str 1, 37085 Göttingen, Germany
    FEBS Lett 559:181-7. 2004
    ..GroEL/GroES thus influences the folding of proteins previously identified as DnaK/TF substrates...
  32. ncbi Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation
    Luis Figueiredo
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    J Biol Chem 279:1090-9. 2004
    ..Additionally, the release of only the folded protein from the GroEL/GroES cage may prevent adverse interactions of the GroEL substrates with the thermosome, which is not normally located within the same compartment...
  33. pmc Error-prone DNA polymerase IV is regulated by the heat shock chaperone GroE in Escherichia coli
    Jill C Layton
    Department of Biology, Indiana University, Jordan Hall, 1001 East Third St, Bloomington, IN 47405, USA
    J Bacteriol 187:449-57. 2005
    ..We were unable to show that GroE interacts directly with Pol IV, suggesting that GroE may act indirectly. Together with previous results, these findings indicate that Pol IV is a component of several cellular stress responses...
  34. ncbi Monitoring macromolecular complexes involved in the chaperonin-assisted protein folding cycle by mass spectrometry
    Esther van Duijn
    Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands
    Nat Methods 2:371-6. 2005
    ..A major advantage of native mass spectrometry is that, given sufficient resolution, it allows the analysis at the picomole level of sensitivity of heterogeneous protein complexes with molecular masses up to several million daltons...
  35. ncbi The architecture of the GroEL-GroES-(ADP)(7) chaperonin complex. II. Heptagrammal characterization of the folding
    A Janner
    Institute for Theoretical Physics, University of Nijmegen, Toernooiveld, 6525 ED Nijmegen, The Netherlands
    Acta Crystallogr D Biol Crystallogr 59:795-808. 2003
    ..The geometric and algebraic restrictions imposed on the indexed positions and on their structural relations by the integrality condition are presented in an appendix...
  36. ncbi Low temperature of GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor DnaK
    S Vorderwülbecke
    Ciphergen Biosystems GmbH, Hannah Vogt Str 1, 37085 Göttingen, Germany
    FEBS Lett 579:181-7. 2005
    ..GroEL/GroES thus influences the folding of proteins previously identified as DnaK/TF substrates...
  37. ncbi Discrimination of ATP, ADP, and AMPPNP by chaperonin GroEL: hexokinase treatment revealed the exclusive role of ATP
    Fumihiro Motojima
    Chemical Resources Laboratory, Tokyo Institute of Technology, 4259 Nagatsuta, Midori ku, Yokohama 226 8503, Japan
    J Biol Chem 278:26648-54. 2003
    ..In the absence of hexokinase, apparent cis folding of rhodanese and malate dehydrogenase was observed in ADP and AMPPNP. Thus, the exclusive role of ATP in generation of the cis ternary complex is now evident...
  38. ncbi Interaction of GroEL and GroEL/GroES complexes with a nonnative subtilisin variant: a small-angle neutron scattering study
    Susan Krueger
    NIST Center for Neutron Research, National Institute of Standards and Technology, 100 Bureau Drive, Stop 8562, Bldg 235 Room E151, Gaithersburg, MD 20899 8562, USA
    J Struct Biol 141:240-58. 2003
    ..However, dPJ9 assumed a more symmetric shape when bound in the GroEL/GroES/dPJ9 complex with ATP. This important observation reflects the relative ability of ATP to promote refolding of protein substrates relative to that of ADP...
  39. ncbi Leu309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroEL
    Ayumi Koike-Takeshita
    Chemical Resources Laboratory, Tokyo Institute of Technology, Midori ku, Yokohama, Japan
    J Biol Chem 281:962-7. 2006
    ..Thus, conformational communication between the two GroES contact sites, the H helix and the GXXLE region (through Leu(309)), appears to play a critical role in encapsulation of the substrate...
  40. ncbi Molecular chaperones--cellular machines for protein folding
    Stefan Walter
    Institut fur Organische Chemie and Biochemie, Technische Universitat Munchen, Lichtenbergstr 4, 85747 Garching, Deutschland
    Angew Chem Int Ed Engl 41:1098-113. 2002
    ..In this review, we discuss the principal features of this peculiar class of proteins, their structure-function relationships, and the underlying molecular mechanisms...
  41. ncbi Encapsulation of an 86-kDa assembly intermediate inside the cavities of GroEL and its single-ring variant SR1 by GroES
    Jiu Li Song
    Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75390, USA
    J Biol Chem 278:2515-21. 2003
    ....
  42. ncbi [Role of GroEL/GroES chaperonin system and Lon protease in regulation of expression Vibrio fischeri lux genes in Escherichia coli cells]
    I V Manukhov
    Mol Biol (Mosk) 40:277-83. 2006
    ..We suppose, that the GroEL/GroES chaperonin systems is required for the folding of LuxR into an active protein, and the LuxR is the target for the ATP-dependent serine Lon protease of E. coli...
  43. ncbi Folding of malate dehydrogenase inside the GroEL-GroES cavity
    J Chen
    Department of Chemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
    Nat Struct Biol 8:721-8. 2001
    ..Moreover, deprotection is broadly distributed throughout MDH, suggesting that it results from breaking hydrogen bonds between MDH and the cavity wall or global destabilization, as opposed to forced mechanical unfolding...
  44. ncbi Effects of divalent cations on encapsulation and release in the GroEL-assisted folding
    Hiroshi Okuda
    Department of Applied Biological Chemistry, School of Agriculture, Kinki University, 3327 204, Nakamachi, Nara, 631 8505, Japan
    Biometals 20:903-10. 2007
    ..SDS-PAGE and gel filtration analyses revealed that cobalt, nickel and zinc ions permit the formation of stable substrate-GroEL-GroES cis-ternary complexes, but prevent the release of METF from GroEL...
  45. ncbi Chaperone mediated solubilization of 69-kDa recombinant maltodextrin glucosidase in Escherichia coli
    S Paul
    Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology Delhi, Hauz Khas, New Delhi, India
    J Appl Microbiol 104:35-41. 2008
    ..To investigate the factors affecting expression and solubilization of Escherichia coli maltodextrin glucosidase in E. coli...
  46. pmc Do chaperonins boost protein yields by accelerating folding or preventing aggregation?
    A I Jewett
    Department of Chemistry and Biochemistry, University of California, Santa Barbara, California, USA
    Biophys J 94:2987-93. 2008
    ....
  47. ncbi Determination of the number of active GroES subunits in the fused heptamer GroES required for interactions with GroEL
    Tatsuya Nojima
    Chemical Resources Laboratory R1 7, Tokyo Institute of Technology, Yokohama, Japan
    J Biol Chem 283:18385-92. 2008
    ..These results indicate the presence of an intermediate GroEL/substrate/GroES complex in which the substrate and GroES bind to GroEL by sharing seven common binding sites...
  48. ncbi Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli
    Ursula Rinas
    Biochemical Engineering Division, GBF German Research Center for Biotechnology, Mascheroder Weg 1, D 38124 Braunschweig, Germany
    J Biotechnol 127:244-57. 2007
    ....
  49. ncbi Co-expression of chaperonin GroEL/GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth characteristics of Escherichia coli
    Parul Gupta
    Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology, Delhi, Hauz Khas, New Delhi 110016, India
    Int J Biochem Cell Biol 38:1975-85. 2006
    ..Optimum in vivo folding of aconitase requires co-production of complete E. coli chaperonin machinery GroEL and GroES together...
  50. ncbi ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells
    J G Thomas
    Department of Chemical Engineering, University of Washington, Seattle 98195, USA
    Mol Microbiol 36:1360-70. 2000
    ..coli cells, presumably by expanding the ability of the DnaK-DnaJ-GrpE team to interact with newly synthesized polypeptides...
  51. ncbi Excluded volume effects on the refolding and assembly of an oligomeric protein. GroEL, a case study
    A Galan
    Unidad de Biofisica (Consejo Superior de Investigaciones Cientificas-Universidad del Pais Vasco (CSIC-UPV)) y Departamento de Bioquimica y Biologia Molecular, Universidad del Pais Vasco, Aptdo. 644, 48080 Bilbao, Spain
    J Biol Chem 276:957-64. 2001
    ..Our data demonstrate that the spontaneous refolding and assembly of homo-oligomeric proteins, such as GroEL, can occur efficiently (70%) under crowding conditions similar to those expected in vivo...
  52. pmc Coexpression of UmuD' with UmuC suppresses the UV mutagenesis deficiency of groE mutants
    C E Donnelly
    Department of Biology, Massachusetts Institute of Technology, Cambridge 02139
    J Bacteriol 174:3133-9. 1992
    ..Instead we found that the presence of UmuD' increased the stability of UmuC in groE strains. In addition, we obtained evidence which indicates that GroEL interacts directly with UmuC...
  53. pmc Molecular analysis of the Haemophilus ducreyi groE heat shock operon
    L M Parsons
    Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany
    Infect Immun 60:4111-8. 1992
    ..Also, H. ducreyi groE mRNA and GroEL were expressed and inducible by heat in E. coli. This is the first report describing the cloning, sequencing, and expression of H. ducreyi protein-encoding genes...
  54. pmc Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli
    A Gragerov
    Institute of Molecular Genetics, Russian Academy of Sciences, Moscow
    Proc Natl Acad Sci U S A 89:10341-4. 1992
    ..Our data suggest that the GroEL and GroES proteins and the DnaK and DnaJ proteins have complementary functions in the folding and assembly of most proteins...
  55. ncbi Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE
    Matthew J Cliff
    Department of Biochemistry, University of Bristol, School of Medical Sciences, UK
    J Biol Chem 281:21266-75. 2006
    ..This ensures efficient encapsulation of the polypeptide within the GroEL central cavity underneath GroES...
  56. pmc Revisiting the GroEL-GroES reaction cycle via the symmetric intermediate implied by novel aspects of the GroEL(D398A) mutant
    Ayumi Koike-Takeshita
    Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa, Chiba, Japan
    J Biol Chem 283:23774-81. 2008
    ..In light of these results, the current model of the GroEL-GroES reaction cycle via the asymmetric 1:1 GroEL-GroES complex deserves reexamination...
  57. ncbi Comparison of refolding activities between nanogel artificial chaperone and GroEL systems
    Wakiko Asayama
    Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University 2 3 10, Kanda Surugadai, Chiyoda ku, Tokyo 101 0062, Japan
    Int J Biol Macromol 42:241-6. 2008
    ..In the nanogel-GFP system, about 90% of the intensity was recovered within 10 min. The half time (t(1/2)) for refolding in the CHP nanogel system (36 s) is almost equal to that of the natural chaperone GroEL-GroES system...
  58. ncbi Molecular cloning of groESL locus, and purification and characterization of chaperonins, GroEL and GroES, from Bacillus brevis
    M Tokunaga
    Laboratory of Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University, Korimoto, Japan
    Biosci Biotechnol Biochem 65:1379-87. 2001
    ..GroEL was estimated to contain 22% alpha-helix, 24% beta-sheet, and 19% turn structures, by CD measurement. GroES protein was also highly purified to examine its chaperonin activity...
  59. ncbi Characterization of heat-shock response of the marine bacterium Vibrio harveyi
    G Klein
    Department of Biochemistry, University of Gdansk, Poland
    Mol Microbiol 16:801-11. 1995
    ..V. harveyi GroES protein had a lower molecular mass (14.5 kDa) than E. coli GroES, migrating in SDS-PAGE as 15kDa protein...
  60. ncbi Structural stability of oligomeric chaperonin 10: the role of two beta-strands at the N and C termini in structural stabilization
    Isao Sakane
    Department of Biotechnology, Faculty of Engineering, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University, Koyama Minami, Tottori 680 8552, Japan
    J Mol Biol 344:1123-33. 2004
    ..From analyses of the mutants' stabilities, it was revealed that the anti-parallel beta-strands at the subunit interface are crucial for subunit association and stabilization of the heptameric GroES protein.
  61. pmc ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate-limiting step of the GroEL/GroES reaction cycle
    Navneet K Tyagi
    Howard Hughes Medical Institute, Department of Genetics, Yale University School of Medicine, Boyer Center, 295 Congress Avenue, New Haven, CT 06510, USA
    FEBS Lett 584:951-3. 2010
    The GroEL/GroES protein folding chamber is formed and dissociated by ATP binding and hydrolysis...
  62. ncbi A study of the antigenicity of Rickettsia helvetica proteins using two-dimensional gel electrophoresis
    Nedaa Hajem
    School of Sustainable Development of Society and Technology, Malardalens University, Eskilstuna, Sweden
    APMIS 117:253-62. 2009
    ..helvetica proteins, three other antigens exist: a 60 kDa GroEL protein, a 10 kDa GroES protein and a hitherto unknown 35 kDa hypothetical protein that has similarities with ORF-RC0799 of Rickettsia conorii...
  63. ncbi The architecture of the GroEL-GroES-(ADP)(7) chaperonin complex. I. Heptagrammal molecular forms
    A Janner
    Institute for Theoretical Physics, University of Nijmegen, Toernooiveld, 6525 ED Nijmegen, The Netherlands
    Acta Crystallogr D Biol Crystallogr 59:783-94. 2003
    ..These forms correspond to a splitting of the monomer into adjacent segments. The change in the folding of the chains in the cis ring of GroEL arising from binding to GroES leaves the chain segmentation invariant...
  64. pmc Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL
    Masatoshi Yokokawa
    Laboratory of Plasma Membrane and Nuclear Signaling, Kyoto University Graduate School of Biostudies, Kyoto, Japan
    EMBO J 25:4567-76. 2006
    ....
  65. pmc GroEL-mediated protein folding: making the impossible, possible
    Zong Lin
    Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA
    Crit Rev Biochem Mol Biol 41:211-39. 2006
    ....
  66. ncbi The aggregation state of rhodanese during folding influences the ability of GroEL to assist reactivation
    A M Bhattacharyya
    Department of Biochemistry, University of Texas Health Science Center, San Antonio, Texas 78229-3900, USA
    J Biol Chem 276:28739-43. 2001
    ..M., McGee, W. A., and Horowitz, P. M. (1998) Biochim. Biophys. Acta 1382, 120--128 and Panda, M., Gorovits, B. M., and Horowitz, P. M. (2000) J. Biol. Chem. 275, 63--70)...
  67. ncbi Chaperone-assisted production of active human Rab8A GTPase in Escherichia coli
    Nathalie Bleimling
    Department of Physical Biochemistry, Max Planck Institute for Molecular Physiology, Otto Hahn Strasse 11, 44227 Dortmund, Germany
    Protein Expr Purif 65:190-5. 2009
    ..The resultant protein was functionally active, as determined by GTPase activity and its interaction with the nucleotide exchange factor MSS4...
  68. ncbi Allostery wiring diagrams in the transitions that drive the GroEL reaction cycle
    RIINA TEHVER
    Biophysics Program, Institute for Physical Science and Technology, University of Maryland, College Park, MD 20742, USA
    J Mol Biol 387:390-406. 2009
    ..We find that several substrate protein binding residues as well as sites related to ATPase activity belong to a single functional network in GroEL. For GroES, the mobile loop residues and GroES/GroES interface residues are linked...
  69. ncbi Comparative immunoproteomics of identification and characterization of virulence factors from Helicobacter pylori related to gastric cancer
    Yu Fen Lin
    Graduate Institute of Biochemistry and Molecular Biology, College of Medicine, National Taiwan University, Taipei 100, Taiwan
    Mol Cell Proteomics 5:1484-96. 2006
    ..We conclude that GroES of H. pylori is a novel GC-associated virulence factor and may contribute to gastric carcinogenesis via induction of inflammation and promotion of cell proliferation...
  70. ncbi Purification and characterization of mouse CYP27B1 overproduced by an Escherichia coli system coexpressing molecular chaperonins GroEL/ES
    Eriko Uchida
    Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kitashirakawa, Oiwake cho, Sakyo ku, Kyoto 606 8502, Japan
    Biochem Biophys Res Commun 323:505-11. 2004
    ..Based on these results and the fact that human CYP27A1 and Streptomyces CYP105A1 also convert vitamin D3 to 1alpha,25(OH)D3, 1alpha-hydroxylation, and 25-hydroxylation of vitamin D3 appear to be closely linked together...
  71. ncbi Single-molecule observation of protein-protein interactions in the chaperonin system
    H Taguchi
    Chemical Resources Laboratory, Tokyo Institute of Technology, 4259 Nagatsuta, Yokohama 226-8503, Japan
    Nat Biotechnol 19:861-5. 2001
    ..However, the release of GroES from GroEL occurred after a lag period ( approximately 3 s) that was not recognized in earlier bulk-phase studies. This observation suggests a new kinetic intermediate in the GroEL-GroES reaction pathway...
  72. ncbi Complex effects of molecular chaperones on the aggregation and refolding of fibroblast growth factor-1
    K L Edwards
    Department of Pharmaceutical Chemistry, University of Kansas, 2095 Constant Avenue, Lawrence, Kansas 66047, USA
    Arch Biochem Biophys 393:14-21. 2001
    ..FGF-1 does, therefore, interact with molecular chaperones, although this may involve both the MG and the native states of the protein...
  73. ncbi Tandem mass spectrometry of intact GroEL-substrate complexes reveals substrate-specific conformational changes in the trans ring
    Esther van Duijn
    Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, The Netherlands
    J Am Chem Soc 128:4694-702. 2006
    ....
  74. ncbi The purification of early-pregnancy factor to homogeneity from human platelets and identification as chaperonin 10
    A C Cavanagh
    Department of Surgery, University of Queensland, Royal Brisbane Hospital, Australia
    Eur J Biochem 222:551-60. 1994
    ..Our studies identify EPF as a member of the highly conserved heat-shock family of molecules and demonstrate a molecular chaperone performing an extracellular role...
  75. ncbi Chaperone-assisted expression, purification, and characterization of recombinant nitrile hydratase NI1 from Comamonas testosteroni
    Julie M Stevens
    Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques UMR 8601 CNRS, Universite Paris V, 45 Rue des Saints Peres, 75270 Paris Cedex 06, France
    Protein Expr Purif 29:70-6. 2003
    ..In addition, we report a rapid and convenient spectrophotometric method to monitor the activity of NI1 NHase during purification...
  76. pmc Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy
    So Yeon Kim
    Department of Chemistry, Stanford University, Stanford, California 94305, USA
    J Phys Chem B 109:24517-25. 2005
    ....
  77. pmc Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins
    O Kandror
    Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA
    EMBO J 14:6021-7. 1995
    ..Thus, TF is a rate-limiting factor for CRAG degradation; it appears to regulate GroEL function and to promote the formation of TF-GroEL-CRAG complexes which are critical for proteolysis...
  78. ncbi GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle
    Takuya Miyazaki
    Department of Biotechnology, Faculty of Engineering, Tottori University, Tottori 680 8552, Japan
    J Biol Chem 277:50621-8. 2002
    ..The behavior of GroEL C138W was reflected closely in its in vivo characteristics, demonstrating the importance of this conformational change to the overall activity of GroEL...
  79. pmc Differential regulation of multiple proteins of Escherichia coli and Salmonella enterica serovar Typhimurium by the transcriptional regulator SlyA
    Andrea Spory
    Lehrstuhl fur Mikrobiologie, Theodor Boveri Institut für Biowissenschaften Biozentrum, Universitat Wurzburg, 97074 Wurzburg, Germany
    J Bacteriol 184:3549-59. 2002
    ..The data suggest that gene regulation by SlyA might be crucial for intracellular survival and/or replication of both EIEC and Salmonella serovar Typhimurium in phagocytic host cells...
  80. pmc Structures of chaperonins from an intracellular symbiont and their functional expression in Escherichia coli groE mutants
    C Ohtaka
    Zoological Institute, Faculty of Science, University of Tokyo, Japan
    J Bacteriol 174:1869-74. 1992
    ..coli groE mutants showed that the chaperonin-10 and chaperonin-60 genes from the endosymbiont are expressed in E. coli and that they can function as molecular chaperones together with endogenous GroEL and GroES, respectively...
  81. pmc The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer
    A Azem
    Department of Botany, Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Israel
    Proc Natl Acad Sci U S A 92:12021-5. 1995
    ..The symmetric heterooligomer behaves as a highly efficient intermediate of the chaperonin protein folding cycle in vitro...
  82. ncbi Isolation, sequence analysis and characterization of a cDNA encoding human chaperonin 10
    J J Chen
    Department of Dermatology, New England Medical Center, Boston, MA 02111
    Biochim Biophys Acta 1219:189-90. 1994
    ..Immunoprecipitation experiment showed that this human cpn10 has an apparent molecular mass of 11 kDa in sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE)...
  83. pmc Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle
    Tomoya Sameshima
    Laboratory of Bio Analytical Chemistry, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7 3 1 Hongo, Bunkyo ku, Tokyo, Japan
    J Biol Chem 283:23765-73. 2008
    ..These results suggest that we should reconsider the chaperonin-mediated protein-folding mechanism that involves the football-shaped complex...
  84. pmc Disulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones
    Eun Sun Park
    Department of Genetics, Yale School of Medicine, New Haven, CT 06510, USA
    Proc Natl Acad Sci U S A 104:2145-50. 2007
    ....
  85. ncbi The intermediate domain defines broad nucleotide selectivity for protein folding in Chlamydophila GroEL1
    Hiroshi Okuda
    Department of Applied Biological Chemistry, School of Agriculture, Kinki University, 3327 204 Nakamachi, Nara, Japan
    J Biol Chem 283:9300-7. 2008
    ..pneumoniae GroEL1 as residues that play a key role in defining the nucleotide selectivity of the protein refolding reaction...
  86. ncbi Chaperonin overexpression promotes genetic variation and enzyme evolution
    Nobuhiko Tokuriki
    Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel
    Nature 459:668-73. 2009
    ..These results indicate that protein stability is a major constraint in protein evolution, and buffering mechanisms such as chaperonins are key in alleviating this constraint...
  87. pmc Chlamydial GroEL autoregulates its own expression through direct interactions with the HrcA repressor protein
    Adam C Wilson
    Department of Microbiology and Molecular Genetics, University of California, Irvine, CA 92697 4025, USA
    J Bacteriol 187:7535-42. 2005
    ..Other chlamydial heat shock proteins, including the two additional GroEL paralogs present in all chlamydial species, did not modulate HrcA activity...
  88. ncbi GroEL walks the fine line: the subtle balance of substrate and co-chaperonin binding by GroEL. A combinatorial investigation by design, selection and screening
    Martin Kawe
    Biochemisches Institut, Universitat Zurich, Winterthurerstrasse 190, CH 8057 Zurich, Switzerland
    J Mol Biol 357:411-26. 2006
    ....
  89. ncbi Absence of classical heat shock response in the citrus pathogen Xylella fastidiosa
    Daniel Martins-de-Souza
    Departamento de Bioquimica, Inst de Biologia, UNICAMP, Campinas, SP, Brazil
    Curr Microbiol 54:119-23. 2007
    ..fastidiosa is related to the absence of a classical stress response, and, probably, alternative strategies for survival of X. fastidiosa under stressfull conditions...
  90. ncbi LocalSCF method for semiempirical quantum-chemical calculation of ultralarge biomolecules
    N A Anikin
    Quantum Biochemistry Group, Konstantina Fedina 3 24, 105215 Moscow, Russian Federation
    J Chem Phys 121:1266-70. 2004
    ..Optimization of linear coefficients of localized orbitals is performed by a gradient procedure. The computer program running on a commodity personal computer was applied to the GroEL-GroES chaperonin complex containing 119,273 atoms...
  91. ncbi The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity
    L Chen
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511, USA
    Cell 99:757-68. 1999
    ..Our structural analysis, combined with other results, suggests that various modes of molecular plasticity are responsible for tight promiscuous binding of nonnative substrates and their release into the shielded cis assembly...
  92. ncbi Expression of active human C1 inhibitor serpin domain in Escherichia coli
    T Lamark
    Institute of Pharmacy, University of Tromsø, Tromsø, 9037, Norway
    Protein Expr Purif 22:349-58. 2001
    ..However, a major obstacle to large-scale production will be to produce the protein in a soluble form. Attempts to increase the yield of soluble protein by coexpression of the GroEL/ES chaperonins resulted in an increase in solubility...
  93. pmc Expression of a highly toxic protein, Bax, in Escherichia coli by attachment of a leader peptide derived from the GroES cochaperone
    M I Donnelly
    Environmental Research Division, Argonne National Laboratory, Argonne, IL 60439, USA
    Protein Expr Purif 22:422-9. 2001
    ..Two-dimensional gel electrophoresis analysis showed that approximately 15-fold more GroES-loop-Bax was produced under these conditions than under standard conditions and that GroEL and DnaK were elevated approximately 3-fold...
  94. ncbi Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
    S C Mande
    Department of Biological Structure, University of Washington, Seattle 98195, USA
    Science 271:203-7. 1996
    ..With the structure of a cpn10 heptamer now revealed and the structure of the E. coli GroEL previously known, models of cpn10:cpn60 and GroEL:GroES complexes are proposed...
  95. ncbi [Archael molecular chaperones: protein folding mechanism of the archael chaperonin]
    Takao Yoshida
    Tanpakushitsu Kakusan Koso 48:33-9. 2003
  96. pmc Effects of reduced levels of GroE chaperones on protein metabolism: enhanced synthesis of heat shock proteins during steady-state growth of Escherichia coli
    M Kanemori
    Institute for Virus Research, Kyoto University, Japan
    J Bacteriol 176:4235-42. 1994
    ....
  97. ncbi Heat shock protein GroE of Escherichia coli: key protective roles against thermal stress
    N Kusukawa
    Institute for Virus Research, Kyoto University, Japan
    Genes Dev 2:874-82. 1988
    ..Thus, GroE plays a key protective role in supporting growth at normal physiological temperatures (20-40 degrees C), whereas high levels of DnaK are required primarily at higher temperature...
  98. ncbi Cloning and disruption of the gene encoding yeast mitochondrial chaperonin 10, the homolog of E. coli groES
    S Rospert
    Biozentrum, University of Basel, Switzerland
    FEBS Lett 335:358-60. 1993
    ..This gene encodes a protein of 11,372 Da that is imported into the mitochondrial matrix without detectable cleavage. Haploid cells lacking a functional copy of CPN10 fail to grow at temperatures between 23 and 37 degrees C...
  99. pmc Mycobacterium tuberculosis chaperonin 10 heptamers self-associate through their biologically active loops
    Michael M Roberts
    Medical Microbiology, Department of Cellular and Molecular Medicine, St George s Hospital Medical School, London SW17 0RE, England
    J Bacteriol 185:4172-85. 2003
    ..Electron density corresponding to a partially disordered protein subunit appears encapsulated within the interior dome cavity of each heptamer. This suggests that the binding of substrates to cpn10 is possible in the absence of cpn60...
  100. pmc A major antigen from Mycobacterium tuberculosis which is homologous to the heat shock proteins groES from E. coli and the htpA gene product of Coxiella burneti
    P N Baird
    Department of Medical Microbiology, London Hospital Medical College, UK
    Nucleic Acids Res 16:9047. 1988
  101. ncbi Isolation and characterization of the groES and groEL genes of Bacillus subtilis Marburg
    Y Tozawa
    Institute of Applied Microbiology, University of Tokyo, Japan
    Biosci Biotechnol Biochem 56:1995-2002. 1992
    ....

Research Grants7

  1. Multiscale Dynamics of Cell Cycle Control and Apoptosis
    Ivet Bahar; Fiscal Year: 2005
    ....
  2. Computational Prediction of Biomolecular Dynamics
    Ivet Bahar; Fiscal Year: 2007
    ..This novel computational methodology will fill a unique niche due to its applicability to large structures and assemblies, its speed and accessibility to the scientific community. ..
  3. MECHANISM OF ACTION OF THE HSP100 CHAPERONE CLPA
    Arthur Horwich; Fiscal Year: 2006
    ....
  4. Chaperonin-mediated protein folding
    Arthur Horwich; Fiscal Year: 2007
    ..unreadable] [unreadable]..
  5. Systems analysis of oxygen regulation in Halobacterium
    AMY SCHMID; Fiscal Year: 2007
    ..These proposed experiments are expected to result in a transcriptional network model that addresses how organisms maintain homeostasis despite stress. [unreadable] [unreadable] [unreadable]..
  6. Computational and experimental studies of targets of protein kinase inhibitors
    ADRIAN HAMILTON ELCOCK; Fiscal Year: 2010
    ..The research proposed here directly addresses the single greatest challenge to the therapeutic pursuit of kinases: how to design small molecule inhibitors that can specifically inhibit a kinase of interest. ..
  7. Molecular Simulations of Folding & Association in Physiological Environments
    ADRIAN HAMILTON ELCOCK; Fiscal Year: 2010
    ..biological and quantitative proteomics data will be utilized to build preliminary 3D models of four different environments in the model prokaryote Escherichia coli: the cytoplasm, periplasm, and inner and outer-membranes ..