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| groel proteinSummarySummary: A chaperonin 60 heat-shock protein isolated from Escherichia coli. Top Publications
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Publications
The crystal structure of the bacterial chaperonin GroEL at 2.8 AK Braig
Department of Genetics, Yale University School of Medicine, Boyer Center, New Haven, Connecticut 06510
Nature 371:578-86. 1994..The three-dimensional structure places most of the mutationally defined functional sites on the channel walls and its outward invaginations, and at the ends of the cylinder...
Coarse-grained normal mode analysis in structural biologyIvet Bahar
Department of Computational Biology, University of Pittsburgh, W1043 Biomedical Science Tower, 200 Lothrop Street, Pittsburgh, PA 15261, USA
Curr Opin Struct Biol 15:586-92. 2005..Such applications have provided great insight into the underlying principles linking protein structures to their dynamics and their dynamics to their functions...
A novel method for detecting intramolecular coevolution: adding a further dimension to selective constraints analysesMario A Fares
Molecular Evolution and Bioinformatics Laboratory, Department of Biology, National University of Ireland, Maynooth, Ireland
Genetics 173:9-23. 2006..All sites detected under adaptive evolution in these proteins belong to coevolution groups, further underlining the importance of testing for coevolution in selective constraints analyses...
Cross-reactive B-cell epitopes of microbial and human heat shock protein 60/65 in atherosclerosisHannes Perschinka
Institute for Biomedical Aging Research, Austrian Academy of Sciences, Peter-Mayr-Strasse 4b, 6020 Innsbruck, Austria
Arterioscler Thromb Vasc Biol 23:1060-5. 2003..These cross-reactive epitopes were shown to serve as autoimmune targets in incipient atherosclerosis and might provide further insights into the mechanisms of early atherogenesis...
Dynamics of allosteric transitions in GroELChangbong Hyeon
Biophysics Program Institute for Physical Science and Technology, Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA
Proc Natl Acad Sci U S A 103:18939-44. 2006..The transition state ensembles (TSEs) connecting the T, R, and R" states are broad with the TSE for the T --> R transition being more plastic than the R --> R" TSE...
Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coliMichael 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...
The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complexZ 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...
Coupling between global dynamics and signal transduction pathways: a mechanism of allostery for chaperonin GroELChakra Chennubhotla
Department of Computational Biology, School of Medicine, University of Pittsburgh, Suite 3064, Pittsburgh, PA 15213, USA
Mol Biosyst 4:287-92. 2008..A functional coupling between the global dynamics sampled under equilibrium conditions and the signal transduction pathways inherently favored by network topology appears to control allosteric effects...
Protein folding: importance of the Anfinsen cageR John Ellis
Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK
Curr Biol 13:R881-3. 2003
The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperaturesO Fayet
Centre de Recherche de Biochimie et Genetique Cellulaires, Centre National de Recherche Scientifique, Toulouse, France
J Bacteriol 171:1379-85. 1989..coli growth and physiology...
Protein folding in the central cavity of the GroEL-GroES chaperonin complexM Mayhew
Cellular Biochemistry and Biophysics Program, Memorial Sloan Kettering Cancer Center, New York, New York 10021, USA
Nature 379:420-6. 1996..Incompletely folded polypeptide rebinds to GroEL, resulting in structural rearrangement for another folding trial in the chaperonin cavity...
Allosteric signaling of ATP hydrolysis in GroEL-GroES complexesNeil A Ranson
Astbury Centre for Structural Molecular Biology and Institute of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, UK
Nat Struct Mol Biol 13:147-52. 2006....
The 13 angstroms structure of a chaperonin GroEL-protein substrate complex by cryo-electron microscopyScott Falke
Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS 66160, USA
J Mol Biol 348:219-30. 2005....
Folding of malate dehydrogenase inside the GroEL-GroES cavityJ 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...
The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coliA 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...
Trigger factor and DnaK cooperate in folding of newly synthesized proteinsE Deuerling
Institut fur Biochemie und Molekularbiologie, Freiburg, Germany
Nature 400:693-6. 1999..Trigger factor and DnaK cooperate to promote proper folding of a variety of E. coli proteins, but neither is essential for folding and viability at intermediate growth temperatures...
GroEL1: a dedicated chaperone involved in mycolic acid biosynthesis during biofilm formation in mycobacteriaAnil Ojha
Pittsburgh Bacteriophage Institute, Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA
Cell 123:861-73. 2005....
Chaperonin-mediated de novo generation of prion protein aggregatesJ 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...
Molecular mechanisms of chaperonin GroEL-GroES functionO 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...
Conversion of the allosteric transition of GroEL from concerted to sequential by the single mutation Asp-155 -> AlaOded Danziger
Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel
Proc Natl Acad Sci U S A 100:13797-802. 2003....
Molecular analysis of the multiple GroEL proteins of ChlamydiaeKaruna P Karunakaran
University of British Columbia Centre for Disease Control. Genome Sequence Centre, British Columbia Cancer Agency, Vancouver, British Columbia, Canada
J Bacteriol 185:1958-66. 2003..coli groEL mutant. Complementation did not occur with groEL2 or groEL3 alone or together with groES. The role for each of the three GroELs in the chlamydial developmental cycle and in disease pathogenesis requires further study...
Directed evolution of substrate-optimized GroEL/S chaperoninsJue 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...
The unfolding action of GroEL on a protein substrateArjan van der Vaart
Institut de Science et d Ingenierie Supramoleculaires, Universite Louis Pasteur, 67000 Strasbourg, France
Biophys J 87:562-73. 2004..The results of the simulation show that multidomain interactions play an essential role, in accord with experiments. Implications of the results for mutation experiments and for the action of GroEL are discussed...
Structure and function of the GroE chaperoneS Walter
Institut fur Organische Chemie and Biochemie, Technische Universitat Munchen, Lichtenbergstr 4, 85747 Garching, Germany
Cell Mol Life Sci 59:1589-97. 2002..Moreover, GroE may actively increase the folding efficiency, e.g. by unfolding of misfolded protein molecules. The mechanisms underlying these features, however, are yet not well characterized...
Phi value analysis of heterogeneity in pathways of allosteric transitions: Evidence for parallel pathways of ATP-induced conformational changes in a GroEL ringAmnon Horovitz
Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel
Proc Natl Acad Sci U S A 99:14095-7. 2002..3. The phi value procedure outlined here should be useful in mapping the energy landscape of allosteric transitions of other proteins...
FtsZ-dependent localization of GroEL protein at possible division sitesHidetaka Ogino
Department of Bioengineering, Tokyo Institute of Technology, 4259 B 38 Nagatsuta, Midori ku, Yokohama 226 8501, Japan
Genes Cells 9:765-71. 2004..The N-terminal amino acid sequence of the protein is identical to that of GroEL protein. Western blotting analysis using anti-GroEL antibody showed that GroEL is indeed concentrated in the vesicles...
Mapping pathways of allosteric communication in GroEL by analysis of correlated mutationsItamar 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...
Structural plasticity and noncovalent substrate binding in the GroEL apical domain. A study using electrospay ionization mass spectrometry and fluorescence binding studiesAlison E Ashcroft
Astbury Centre for Structural Molecular Biology and School of Biochemistry and Molecular Biology, The University of Leeds, Leeds LS2 9JT, United Kingdom
J Biol Chem 277:33115-26. 2002....
Phylogenetic classification of Bartonella species by comparing groEL sequencesZaher Zeaiter
Unite des Rickettsies, CNRS UPRES A 6020, Faculte de Medecine, Marseille, France
Int J Syst Evol Microbiol 52:165-71. 2002..In addition, the groEL gene was shown to be useful in subtyping six B. henselae isolates into three variants: Houston, Marseille and Fizz...
Isolation and characterisation of mutants of GroEL that are fully functional as single ringsZhe Sun
School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK
J Mol Biol 332:715-28. 2003..These active single rings should provide a useful tool for studying the nature of the allosteric changes that occur in the GroEL reaction cycle...
Translocation boost protein-folding efficiency of double-barreled chaperoninsIvan 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...
An expanded protein folding cage in the GroEL-gp31 complexDaniel 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...
Fitting low-resolution cryo-EM maps of proteins using constrained geometric simulationsCraig C Jolley
Center for Biological Physics, Bateman Physical Sciences, Arizona State University, Tempe, Arizona, USA
Biophys J 94:1613-21. 2008..We show that by incorporating the correct local stereochemistry in the modeling, structures can be obtained with effective resolution that is significantly higher than might be expected from the nominal cryo-EM resolution...
Residues in chaperonin GroEL required for polypeptide binding and releaseW 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...
Allosteric transitions in the chaperonin GroEL are captured by a dominant normal mode that is most robust to sequence variationsWenjun Zheng
Laboratory of Computational Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland, USA
Biophys J 93:2289-99. 2007..Many of these residues are located in intersubunit interfaces, and may therefore play a critical role in transmitting allosteric signals between subunits...
Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated proteinYun-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...
A thermodynamic coupling mechanism for GroEL-mediated unfoldingS Walter
Laboratorium fur Biochemie, Universitat Bayreuth, Germany
Proc Natl Acad Sci U S A 93:9425-30. 1996....
Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolutionK Braig
Department of Genetics, Yale University, New Haven, Connecticut 06510, USA
Nat Struct Biol 2:1083-94. 1995..The variability of these regions may play a role in the ability of GroEL to bind a wide variety of substrates...
Low-frequency normal modes that describe allosteric transitions in biological nanomachines are robust to sequence variationsWenjun Zheng
Laboratory of Computational Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA
Proc Natl Acad Sci U S A 103:7664-9. 2006..Our work shows that robustness of dynamical modes at the mesoscopic level is encoded in the structure through a sparse network of residues that transmit allosteric signals...
The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversityL 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...
A conservative test of genetic drift in the endosymbiotic bacterium Buchnera: slightly deleterious mutations in the chaperonin groELJoshua T Herbeck
Josephine Bay Paul Center for Comparative Molecular Biology and Evolution, Marine Biological Laboratory, Woods Hole, Massachusetts 02543, USA
Genetics 165:1651-60. 2003..Rather, they further support the hypothesis that drift is an important force driving accelerated protein evolution in this obligate mutualist...
Expansion and compression of a protein folding intermediate by GroELZong Lin
Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA
Mol Cell 16:23-34. 2004....
A mobile loop order-disorder transition modulates the speed of chaperonin cyclingFrank 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...
Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroEMatthew 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...
Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energeticsCharu 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...
Characterization of the groEL and groES loci in Bifidobacterium breve UCC 2003: genetic, transcriptional, and phylogenetic analysesMarco Ventura
Department of Microbiology, National University of Ireland, Western Road, Cork, Ireland
Appl Environ Microbiol 70:6197-209. 2004....
A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociationB 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...
Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coliN Kusukawa
Institute for Virus Research, Kyoto University, Japan
EMBO J 8:3517-21. 1989..The translocation of other secretory proteins, however, appears to depend minimally on GroE, suggesting that GroE interacts only with a specific class of secreted proteins...
ATP-bound states of GroEL captured by cryo-electron microscopyN A Ranson
Department of Crystallography, Birkbeck College London, Malet Street, London WC1E 7HX, United Kingdom
Cell 107:869-79. 2001..The model for cooperativity, based on switching of intersubunit salt bridge interactions around the GroEL ring, may provide general insight into cooperativity in other ring complexes and molecular machines...
The chaperonins of Synechocystis PCC 6803 differ in heat inducibility and chaperone activityE Kovacs
Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences, Szeged, H 6701, Hungary
Biochem Biophys Res Commun 289:908-15. 2001..The difference in chaperone activity of the two cyanobacterial chaperonins very probably reflects the unique chaperonin properties required during the life of Synechocystis PCC 6803...
A structural model for GroEL-polypeptide recognitionA M Buckle
Cambridge University Chemical Laboratory, Medical Research Council Centre, United Kingdom
Proc Natl Acad Sci U S A 94:3571-5. 1997..A ring of connected binding sites is noted that can explain many aspects of substrate binding and activity...
Annealing function of GroEL: structural and bioinformatic analysisGeorge Stan
Laboratory of Biophysical Chemistry, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA
Biophys Chem 100:453-67. 2003..This leads to the prediction that mutating these residues, that control the annealing function of the SP, can decrease the efficacy of the chaperonin function...
Allosteric regulation of chaperoninsAmnon Horovitz
Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel
Curr Opin Struct Biol 15:646-51. 2005..However, various mechanistic issues remain to be resolved...
Direct NMR observation of a substrate protein bound to the chaperonin GroELReto Horst
Institut fur Molekularbiologie und Biophysik, Eidgenossische Technische Hochschule Zurich, CH 8093 Zurich, Switzerland
Proc Natl Acad Sci U S A 102:12748-53. 2005..The NMR data suggest that the bound state includes random coil conformations devoid of stable native-like tertiary contacts and that the bound hDHFR might best be described as a dynamic ensemble of randomly structured conformers...
Revisiting the GroEL-GroES reaction cycle via the symmetric intermediate implied by novel aspects of the GroEL(D398A) mutantAyumi 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...
Chaperone mediated solubilization of 69-kDa recombinant maltodextrin glucosidase in Escherichia coliS 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...
Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solutionReto Horst
Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
Proc Natl Acad Sci U S A 104:20788-92. 2007....
Determination of the number of active GroES subunits in the fused heptamer GroES required for interactions with GroELTatsuya 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...
Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulationLuis 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...
Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaKS 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...
Mechanisms of ATPases--a multi-disciplinary approachMathieu 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...
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....
GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycleTakuya 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...
Comparison of refolding activities between nanogel artificial chaperone and GroEL systemsWakiko 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...
DnaK and DnaJ facilitated the folding process and reduced inclusion body formation of magnesium transporter CorA overexpressed in Escherichia coliYong 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...
Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate statesCharu Chaudhry
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA
J Mol Biol 342:229-45. 2004....
Co-expression of chaperonin GroEL/GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth characteristics of Escherichia coliParul 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...
Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopySo Yeon Kim
Department of Chemistry, Stanford University, Stanford, California 94305, USA
J Phys Chem B 109:24517-25. 2005....
Expression, purification, and characterization of a novel recombinant fusion protein, rhTPO/SCF, in Escherichia coliYuhui 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...
Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperonesArio de Marco
Protein Expression Unit, European Molecular Biology Laboratory, Heidelberg, Germany
Cell Stress Chaperones 10:329-39. 2005....
Leu309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroELAyumi 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...
Coexpression of UmuD' with UmuC suppresses the UV mutagenesis deficiency of groE mutantsC 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...
Co-translational binding of GroEL to nascent polypeptides is followed by post-translational encapsulation by GroES to mediate protein foldingBei Wen Ying
Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, FSB 401, 5 1 5 Kashiwanoha, Kashiwa, Chiba 277 8562, Japan
J Biol Chem 281:21813-9. 2006..GroEL holds the nascent chain on the ribosome in a polypeptide length-dependent manner and post-translationally encapsulates the polypeptide using the GroES cap to accomplish the chaperonin-mediated folding process...
Low temperature of GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor DnaKS 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...
Chaperonin GroEL meets the substrate protein as a "load" of the ringsHideki Taguchi
Graduate School of Frontier Sciences, University of Tokyo
J Biochem 137:543-9. 2005..Finally I propose the mechanistic similarity between GroEL and kinesin, a molecular motor that moves along a microtubule in an ATP-dependent manner...
Factors governing the substrate recognition by GroEL chaperone: a sequence correlation approachTapan 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....
Error-prone DNA polymerase IV is regulated by the heat shock chaperone GroE in Escherichia coliJill 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...
Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coliUrsula Rinas
Biochemical Engineering Division, GBF German Research Center for Biotechnology, Mascheroder Weg 1, D 38124 Braunschweig, Germany
J Biotechnol 127:244-57. 2007....
Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroELMasatoshi Yokokawa
Laboratory of Plasma Membrane and Nuclear Signaling, Kyoto University Graduate School of Biostudies, Kyoto, Japan
EMBO J 25:4567-76. 2006....
Effects of divalent cations on encapsulation and release in the GroEL-assisted foldingHiroshi 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...
The 69 kDa Escherichia coli maltodextrin glucosidase does not get encapsulated underneath GroES and folds through trans mechanism during GroEL/GroES-assisted foldingSubhankar Paul
Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology Delhi, Hauz Khas, New Delhi 110016, India
FASEB J 21:2874-85. 2007..GroES could not encapsulate GroEL-bound MalZ. All these experimental findings suggested that GroEL/GroES-assisted folding of MalZ followed trans mechanism, whereas denatured MalZ and GroES bound to the opposite rings of a GroEL molecule...
[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...
Molecular chaperones--cellular machines for protein foldingStefan Walter
, , 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...
GroEL interacts transiently with oxidatively inactivated rhodanese facilitating its reactivationGirish C Melkani
Department of Chemistry and Biochemistry, California State University at San Marcos, 92096-0001, USA
Biochem Biophys Res Commun 294:893-9. 2002....
Machinery of protein folding and unfoldingXiaodong 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...
ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cellsJ 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...
Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroESJ Martin
Cellular Biochemistry and Biophysics Program, Memorial Sloan Kettering Cancer Center, New York 10021
Nature 366:279-82. 1993..ATP binding to GroES may be important in charging the seven subunits of the interacting GroEL ring with ATP to facilitate cooperative ATP binding and hydrolysis for substrate protein release...
Assembly of chaperonin complexesA 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...
Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteinsO 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...
Purification and characterization of the GroESLx chaperonins from the symbiotic X-bacteria in Amoeba proteusG 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...
The ins and outs of GroEL-mediated protein foldingJ 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...
GroEL/GroES-mediated folding of a protein too large to be encapsulatedT 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...
Dual function of protein confinement in chaperonin-assisted protein foldingA Brinker
Department of Cellular Biochemistry, Max-Planck-Institute of Biochemistry, 82152 Martinsried, Germany
Cell 107:223-33. 2001....
Distinct actions of cis and trans ATP within the double ring of the chaperonin GroELH S Rye
Howard Hughes Medical Institute, Department of Genetics, School of Medicine, Yale University, New Haven, Connecticut 06510, USA
Nature 388:792-8. 1997..These observations offer an explanation of why GroEL functions as a double-ring complex...
Complex effects of molecular chaperones on the aggregation and refolding of fibroblast growth factor-1K 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...
Excluded volume effects on the refolding and assembly of an oligomeric protein. GroEL, a case studyA 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...
Isolation and analysis of mutant alleles of the Bacillus subtilis HrcA repressor with reduced dependency on GroE functionSilke 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...
Molecular analysis of the Haemophilus ducreyi groE heat shock operonL 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...
Coexistence of group I and group II chaperonins in the archaeon Methanosarcina mazeiDaniel Klunker
Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, 82152 Martinsried, Germany
J Biol Chem 278:33256-67. 2003....
The architecture of the GroEL-GroES-(ADP)(7) chaperonin complex. II. Heptagrammal characterization of the foldingA 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...
Discrimination of ATP, ADP, and AMPPNP by chaperonin GroEL: hexokinase treatment revealed the exclusive role of ATPFumihiro 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...
Research Grants
- TARGETING OF HUMAN OTC TO THE MITOCHONDRIAL MATRIXArthur Horwich; Fiscal Year: 1992..In vitro synthesized precursors with either reactive amino acid side chains or enzymatically active mature portions will also be used as affinity- labeling reagents, to identify additional interacting mitochondrial components...
- Chaperonin-mediated protein foldingArthur Horwich; Fiscal Year: 2007....
- MECHANISM OF ACTION OF THE HSP100 CHAPERONE CLPAArthur Horwich; Fiscal Year: 2006....
- GROEL-MEDIATED PROTEIN FOLDINGArthur Horwich; Fiscal Year: 2000..I.'s laboratory, in conjunction with GroEL-mutant "traps" that are capable of binding but not releasing non-native polypeptides, will be used to test these hypotheses. ..
- FUNCTION OF GROEL IN THE BACTERIAL CYTOPLASMArthur Horwich; Fiscal Year: 1993....
- Engineering Microbial Rhodopsins as Optical Voltage SensorsADAM EZRA COHEN; Fiscal Year: 2011..This protein will facilitate studies on the electrophysiology of a wide range of cells implicated in human health and disease. ..
- Multiscale Dynamics of Cell Cycle Control and ApoptosisIvet Bahar; Fiscal Year: 2005....
- Computational approaches to single molecule force spectroscopyDEVARAJAN THIRUMALAI THIRUMALAI; Fiscal Year: 2010..The studies will give us insights into diseases linked to misfolding and the biophysical basis of response of cell adhesion proteins to inflammation and tissue injury. ..
- Sensor Technology for Rapid Microbial Identification and Susceptibility TestingDavid Haake; Fiscal Year: 2007..As described in the Product Development Plan, these studies will position our industrial partner, GeneFluidics, for near-term deployment of the PATHOSENSE instrument in multiple clinical settings. ..
- Hemin Receptor Gene Family of Bartonella quintanaMICHAEL MINNICK; Fiscal Year: 2006..abstract_text> ..
- Comparison of Human Ehrlichiosis Agent GenomesYasuko Rikihisa; Fiscal Year: 2007..chaffeensis virulence determinants and their pathogenic mechanisms. The results may point to potential chemotherapy, chemopreventive and/or vaccine candidates for treatment and prevention of human ehrlichiosis. ..
- Conformational Change in Molecular BiologyMartin Karplus; Fiscal Year: 2009..We will study how these motors work and employ the results to find inhibitors for ATP synthesis in the mitochondria, a suggested treatment of cancer, and to interpret the effect of replication errors in DNA synthesis by polymerases. ..
- OUTER MEMBRANE PROTEINS OF PATHOGENIC LEPTOSPIRA SPECIESDavid Haake; Fiscal Year: 2007..We will examine the mechanism(s) by which antibodies to osmo-upregulated OMPs mediate protection using assays of bactericidal activity, growth inhibition, opsonophagocytosis, and adherence inhibition. ..
- Conformational Change in Molecular BiologyMartin Karplus; Fiscal Year: 2010..We will study how these motors work and employ the results to find inhibitors for ATP synthesis in the mitochondria, a suggested treatment of cancer, and to interpret the effect of replication errors in DNA synthesis by polymerases. ..
- Structural Dynamics of Biomolecular SystemsIvet Bahar; Fiscal Year: 2010..abstract_text> ..
- Comparison of Human Ehrlichiosis Agent GenomesYasuko Rikihisa; Fiscal Year: 2010..chaffeensis virulence determinants and their pathogenic mechanisms. The results may point to potential chemotherapy, chemopreventive and/or vaccine candidates for treatment and prevention of human ehrlichiosis. ..
- Hemin Receptor Gene Family of Bartonella quintanaMICHAEL MINNICK; Fiscal Year: 2003..Further, since Bartonella Hbp's are possibly members of an outer membrane protein family from several Gram-negative bacteria, data generated from this study will undoubtedly be of broad importance to bacterial pathogenesis. ..
- EHRLICHIACIDAL MECHANISM BY LEUKOCYTESYasuko Rikihisa; Fiscal Year: 2003..The knowledge will be exploited in identifying novel therapeutic and vaccine targets. ..
- PROTEIN FOLDING DYNAMICS BY MASS SPECTROMETRYIGOR KALTASHOV; Fiscal Year: 2004..The proposed studies will significantly further our understanding of the protein folding processes and the mechanisms by which transport proteins function in vivo. ..
- ROLES OF EHRLICHIAL OUTER MEMBRANE PROTEIN IN PARASITISMYasuko Rikihisa; Fiscal Year: 2001..Aim 5 addresses hypothesis 3 by examining the effects of immunization with the ehrlichial OMP in a mouse model of human ehrlichiosis. ..
- Bartonella Inhibitory Factor for Endothelial Cell GrowthMICHAEL MINNICK; Fiscal Year: 2002..abstract_text> ..
- Computational and experimental studies of targets of protein kinase inhibitorsADRIAN ELCOCK; Fiscal Year: 2007..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. ..
- Conformational Change in Molecular BiologyMartin Karplus; Fiscal Year: 2006..We will study how these motors work and employ the results to find inhibitors for ATP synthesis in the mitochondria, a suggested treatment of cancer, and to interpret the effect of replication errors in DNA synthesis by polymerases. ..
- COMPARISON OF 3 HUMAN EHRLICHIOSIS GENOME SEQUENCESYasuko Rikihisa; Fiscal Year: 2002....
- Investigation of protein dynamics by mass spectrometryIGOR KALTASHOV; Fiscal Year: 2009....
- GENE EXPRESSION BY HUMAN GRANULOCYTIC EHRLICHIOSIS AGYasuko Rikihisa; Fiscal Year: 2004..These efforts are expected to reveal an important role for the p44-multigene family in strategies of adaptive surface variation and avoidance of host immune responses. ..
- Alignment-independent Classification of ProteinsIvet Bahar; Fiscal Year: 2007....
- Structural Dynamics of Biomolecular SystemsIvet Bahar; Fiscal Year: 2009..These aims will be pursued in collaboration with the National Center for Biomedical Computing Simbios at Stanford U. ..
