Gene Symbol: groS
Description: Cpn10 chaperonin GroES, small subunit of GroESL
Alias: ECK4136, JW4102, TabB, groES, mopB
Species: Escherichia coli str. K-12 substr. MG1655
Products:     groS

Top Publications

  1. Janner A. Hidden order in the GroEL-GroES-(ADP)7 chaperonin: forms, folding, and ADP-binding sites. Proteins. 2003;51:126-36 pubmed
    A molecular crystallography approach reveals the existence of a hidden order in GroEL-GroES-(ADP)(7). The new crystallographic symmetry concepts required are first illustrated for a hypothetical planar molecule...
  2. Walter S. Structure and function of the GroE chaperone. Cell Mol Life Sci. 2002;59:1589-97 pubmed
    The Escherichia coli proteins GroEL and GroES were the first chaperones to be studied in detail and have thus become a role model for assisted protein folding in general...
  3. Graubner W, Schierhorn A, Brüser T. DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone. J Biol Chem. 2007;282:7116-24 pubmed
    ..The overall results suggest that SlyD and DnaK are in the set of chaperones that can serve as general Tat signal-binding proteins. DnaK has additional functions that are indispensable for the targeting of CueO. ..
  4. El Hage A, Sbai M, Alix J. The chaperonin GroEL and other heat-shock proteins, besides DnaK, participate in ribosome biogenesis in Escherichia coli. Mol Gen Genet. 2001;264:796-808 pubmed
    ..Interestingly, overproduction of GroES/GroEL can partially compensate for a lack of DnaK/DnaJ at 44 degrees C.
  5. Neidhardt F, Phillips T, VanBogelen R, Smith M, Georgalis Y, Subramanian A. Identity of the B56.5 protein, the A-protein, and the groE gene product of Escherichia coli. J Bacteriol. 1981;145:513-20 pubmed
    ..5 has now been shown to be the groE gene product and to be identical with the A-protein. ..
  6. Vorderwülbecke S, Kramer G, Merz F, Kurz T, Rauch T, Zachmann Brand B, et al. Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK. FEBS Lett. 2004;559:181-7 pubmed
    ..of DeltatigDeltadnaK52 cells is abrogated either by growth below 30 degrees C or by overproduction of GroEL/GroES. At 23 degrees C DeltatigDeltadnaK52 cells were viable and showed only minor protein aggregation...
  7. Miyazaki T, Yoshimi T, Furutsu Y, Hongo K, Mizobata T, Kanemori M, et al. GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle. J Biol Chem. 2002;277:50621-8 pubmed
    ..form of Escherichia coli GroEL, which forms an arrested ternary complex composed of GroEL, the co-chaperonin GroES and the refolding protein molecule rhodanese at 25 degrees C...
  8. Kusukawa N, Yura T. Heat shock protein GroE of Escherichia coli: key protective roles against thermal stress. Genes Dev. 1988;2:874-82 pubmed
    ..a DNA insertion in the groE upstream region, resulting in high-level synthesis of major heat shock proteins GroE (GroES and GroEL)...
  9. Taglicht D, Padan E, Oppenheim A, Schuldiner S. An alkaline shift induces the heat shock response in Escherichia coli. J Bacteriol. 1987;169:885-7 pubmed
    ..An acidic shift of extracellular pH failed to activate the heat shock response, showing that the response is specific to the alkaline shift. ..

More Information


  1. Buchberger A, Schroder H, Hesterkamp T, Schönfeld H, Bukau B. Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding. J Mol Biol. 1996;261:328-33 pubmed
    ..particular importance for the assisted refolding of proteins that are unfolded by stress treatment such as heat shock and whose size is too large to allow folding inside the substrate binding cavity of the GroEL ring underneath GroES.
  2. Nojima T, Murayama S, Yoshida M, Motojima F. Determination of the number of active GroES subunits in the fused heptamer GroES required for interactions with GroEL. J Biol Chem. 2008;283:18385-92 pubmed publisher
    A double-heptamer ring chaperonin GroEL binds denatured substrate protein, ATP, and GroES to the same heptamer ring and encapsulates substrate into the central cavity underneath GroES where productive folding occurs...
  3. Brocchieri L, Karlin S. Conservation among HSP60 sequences in relation to structure, function, and evolution. Protein Sci. 2000;9:476-86 pubmed
    ..diverse HSP60 sequences, centering on ATP/ADP and Mg2+ binding sites, on residues interacting with substrate, on GroES contact positions, on interface regions between monomers and domains, and on residues important in allosteric ..
  4. Kerner M, Naylor D, Ishihama Y, Maier T, Chang H, Stines A, et al. Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell. 2005;122:209-20 pubmed
    The E. coli chaperonin GroEL and its cofactor GroES promote protein folding by sequestering nonnative polypeptides in a cage-like structure. Here we define the contribution of this system to protein folding across the entire E...
  5. Strocchi M, Ferrer M, Timmis K, Golyshin P. Low temperature-induced systems failure in Escherichia coli: insights from rescue by cold-adapted chaperones. Proteomics. 2006;6:193-206 pubmed
    ..coli cells at low temperatures. ..
  6. McLennan N, Masters M. GroE is vital for cell-wall synthesis. Nature. 1998;392:139 pubmed
  7. Amatore D, Baneyx F. Insertion mutagenesis of Escherichiacoli GroEL. Biochem Biophys Res Commun. 2003;302:246-52 pubmed
    ..inactive as minichaperones as they failed to restore the growth of groEL140 cells at 43 degrees C whether or not GroES was co-expressed. A 31-residue insertion in equatorial helix D led to complete degradation of GroEL90...
  8. Kanemori M, Mori H, Yura T. Effects of reduced levels of GroE chaperones on protein metabolism: enhanced synthesis of heat shock proteins during steady-state growth of Escherichia coli. J Bacteriol. 1994;176:4235-42 pubmed
    The GroE heat shock proteins (GroEL and GroES) of Escherichia coli represent major molecular chaperones that participate in folding (and assembly) of a variety of proteins and are essential for cell growth at all temperatures...
  9. Inobe T, Arai M, Nakao M, Ito K, Kamagata K, Makio T, et al. Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy. J Mol Biol. 2003;327:183-91 pubmed
  10. Horwich A, Low K, Fenton W, Hirshfield I, Furtak K. Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell. 1993;74:909-17 pubmed
    ..We conclude that GroEL indeed is a machine at the distal end of the pathway of transfer of genetic information, assisting a large and specific set of newly translated cytoplasmic proteins to reach their native tertiary structures...
  11. Chaudhuri T, Verma V, Maheshwari A. GroEL assisted folding of large polypeptide substrates in Escherichia coli: Present scenario and assignments for the future. Prog Biophys Mol Biol. 2009;99:42-50 pubmed publisher
    Escherichia coli chaperonins GroEL and GroES are indispensable for survival and growth of the cell since they provide essential assistance to the folding of many newly translated proteins in the cell...
  12. Chen D, Madan D, Weaver J, Lin Z, Schr der G, Chiu W, et al. Visualizing GroEL/ES in the act of encapsulating a folding protein. Cell. 2013;153:1354-65 pubmed publisher
    ..How these substrate proteins are encapsulated within the GroEL-GroES cavity is poorly understood...
  13. Saint Ruf C, Taddei F, Matic I. Stress and survival of aging Escherichia coli rpoS colonies. Genetics. 2004;168:541-6 pubmed
    ..By measuring cell viability and by transcriptome analysis, here we show that rpoS cells as well as wild-type cells survive when they form colonies on solid media. ..
  14. Ying B, Taguchi H, Ueda T. Co-translational binding of GroEL to nascent polypeptides is followed by post-translational encapsulation by GroES to mediate protein folding. J Biol Chem. 2006;281:21813-9 pubmed
    The eubacterial chaperonins GroEL and GroES are essential chaperones and primarily assist protein folding in the cell...
  15. Stan G, Brooks B, Lorimer G, Thirumalai D. Identifying natural substrates for chaperonins using a sequence-based approach. Protein Sci. 2005;14:193-201 pubmed
    ..on the hypothesis that natural SPs are those that contain patterns of residues similar to those found in either GroES mobile loop and/or strongly binding peptide in complex with GroEL...
  16. Lenz G, Ron E. Novel interaction between the major bacterial heat shock chaperone (GroESL) and an RNA chaperone (CspC). J Mol Biol. 2014;426:460-6 pubmed publisher
    ..One of the major heat shock chaperones in Escherichia coli is GroESL, composed of GroES and GroEL (the bacterial Hsp10 and Hsp60 homologues), which is essential for refolding of misfolded proteins...
  17. Chuang S, Blattner F. Characterization of twenty-six new heat shock genes of Escherichia coli. J Bacteriol. 1993;175:5242-52 pubmed
    ..were found to be similar to those of the four most studied heat shock proteins, DnaK, DnaJ, GroEL (MopA), and GroES (MopB)...
  18. Kubo T, Mizobata T, Kawata Y. Refolding of yeast enolase in the presence of the chaperonin GroE. The nucleotide specificity of GroE and the role of GroES. J Biol Chem. 1993;268:19346-51 pubmed
    ..The specific mechanism of GroE-facilitated folding involves numerous interactions between GroEL, GroES, the refolding protein, and ATP...
  19. Wang J, Herman C, Tipton K, Gross C, Weissman J. Directed evolution of substrate-optimized GroEL/S chaperonins. Cell. 2002;111:1027-39 pubmed
    ..This conflict and the nature of the ring structure may help explain the evolution of cellular chaperone systems. ..
  20. Gaitanaris G, Vysokanov A, Hung S, Gottesman M, Gragerov A. Successive action of Escherichia coli chaperones in vivo. Mol Microbiol. 1994;14:861-9 pubmed
    ..1990). Here we demonstrate that in addition to the above three proteins, GroEL and GroES are necessary for the Cl857 repressor to acquire full activity at the permissive temperature...
  21. Schiener J, Witt S, Hayer Hartl M, Guckenberger R. How to orient the functional GroEL-SR1 mutant for atomic force microscopy investigations. Biochem Biophys Res Commun. 2005;328:477-83 pubmed
    ..of GroEL with its simplified composition, but unaltered capability of binding substrates and the co-chaperone GroES, is a more suited system for AFM studies...
  22. Kovacs E, Sun Z, Liu H, Scott D, Karsisiotis A, Clarke A, et al. Characterisation of a GroEL single-ring mutant that supports growth of Escherichia coli and has GroES-dependent ATPase activity. J Mol Biol. 2010;396:1271-83 pubmed publisher
    ..The association of ATP and GroES to a polypeptide-bound ring of GroEL encapsulates the folding proteins in the central cavity of that ring (cis ..
  23. Blennow A, Surin B, Ehring H, McLennan N, Spangfort M. Isolation and biochemical characterization of highly purified Escherichia coli molecular chaperone Cpn60 (GroEL) by affinity chromatography and urea-induced monomerization. Biochim Biophys Acta. 1995;1252:69-78 pubmed
    ..By use of MALDI-MS, highly accurate molecular masses of wild-type and a truncated form of GroEL were determined and verified, by comparison with their respective gene sequences. ..
  24. Karplus M, Gao Y, Ma J, van der Vaart A, Yang W. Protein structural transitions and their functional role. Philos Trans A Math Phys Eng Sci. 2005;363:331-55; discussion 355-6 pubmed
    ..In this paper we outline our studies of two such protein machines. One is GroEL, the chaperone from Escherichia coli, which aids in protein folding; the other is F(1)-ATPase, a motor protein which synthesizes and hydrolyses ATP. ..
  25. Hendrix R. Purification and properties of groE, a host protein involved in bacteriophage assembly. J Mol Biol. 1979;129:375-92 pubmed
  26. Goloubinoff P, Christeller J, Gatenby A, Lorimer G. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP. Nature. 1989;342:884-9 pubmed
    ..coli (groES), and Mg-ATP...
  27. Chen D, Luke K, Zhang J, Chiu W, Wittung Stafshede P. Location and flexibility of the unique C-terminal tail of Aquifex aeolicus co-chaperonin protein 10 as derived by cryo-electron microscopy and biophysical techniques. J Mol Biol. 2008;381:707-17 pubmed publisher
    Co-chaperonin protein 10 (cpn10, GroES in Escherichia coli) is a ring-shaped heptameric protein that facilitates substrate folding when in complex with cpn60 (GroEL in E. coli)...
  28. Yokokawa M, Wada C, Ando T, Sakai N, Yagi A, Yoshimura S, et al. Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL. EMBO J. 2006;25:4567-76 pubmed
    In order to fold non-native proteins, chaperonin GroEL undergoes numerous conformational changes and GroES binding in the ATP-dependent reaction cycle...
  29. Laminet A, Ziegelhoffer T, Georgopoulos C, Pluckthun A. The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor. EMBO J. 1990;9:2315-9 pubmed
    ..Purified GroES alone has no effect on folding...
  30. Nam S, Walsh M. Characterization of interactions between Escherichia coli molecular chaperones and immobilized caseins. Prep Biochem Biotechnol. 2003;33:321-39 pubmed
    ..Western analysis identified five E. coli molecular chaperones including DnaK, DnaJ, GrpE, GroEL, and GroES in eluates...
  31. Tilly K, Murialdo H, Georgopoulos C. Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis. Proc Natl Acad Sci U S A. 1981;78:1629-33 pubmed
    ..One groE gene, groEL, has been shown to encode the synthesis of a 65,000 Mr polypeptide, whereas the second, groES, codes for the synthesis of a 15,000 Mr polypeptide...
  32. Higurashi T, Yagi H, Mizobata T, Kawata Y. Amyloid-like fibril formation of co-chaperonin GroES: nucleation and extension prefer different degrees of molecular compactness. J Mol Biol. 2005;351:1057-69 pubmed
    The molecular chaperone GroES, together with GroEL from Escherichia coli, is the best characterized protein of the molecular chaperone family...
  33. Braig K, Otwinowski Z, Hegde R, Boisvert D, Joachimiak A, Horwich A, et al. The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature. 1994;371:578-86 pubmed
    ..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. ..
  34. Motojima F, Yoshida M. Discrimination of ATP, ADP, and AMPPNP by chaperonin GroEL: hexokinase treatment revealed the exclusive role of ATP. J Biol Chem. 2003;278:26648-54 pubmed
    The double ring chaperonin GroEL binds unfolded protein, ATP, and GroES to the same ring, generating the cis ternary complex in which folding occurs within the cavity capped by GroES (cis folding)...
  35. Xu Z, Horwich A, Sigler P. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature. 1997;388:741-50 pubmed
    ..In Escherichia coli, asymmetric intermediates of GroEL are formed with the co-chaperonin GroES and nucleotides bound only to one of the seven-subunit rings (the cis ring) and not to the opposing ring (the ..
  36. Lund P. Microbial molecular chaperones. Adv Microb Physiol. 2001;44:93-140 pubmed
    ..Other examples of regulation of molecular chaperones will also be discussed. Finally, the likely future research directions for molecular chaperone biology in the post-genomic era will be briefly evaluated. ..
  37. Yano R, Imai M, Yura T. The use of operon fusions in studies of the heat-shock response: effects of altered sigma 32 on heat-shock promoter function in Escherichia coli. Mol Gen Genet. 1987;207:24-8 pubmed
    ..In some instances, the response was significantly delayed. These results point to the usefulness of the lambda pF13-derivative phages for quantitative and systematic analysis of heat-shock response in E. coli. ..
  38. Illingworth M, Ramsey A, Zheng Z, Chen L. Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES. J Biol Chem. 2011;286:30401-8 pubmed publisher
    In mediating protein folding, chaperonin GroEL and cochaperonin GroES form an enclosed chamber for substrate proteins in an ATP-dependent manner...
  39. Laskowska E, Kuczynska Wisnik D, Bak M, Lipinska B. Trimethoprim induces heat shock proteins and protein aggregation in E. coli cells. Curr Microbiol. 2003;47:286-9 pubmed
    ..Upon folate stress, deletion of the delta ibpA/B operon resulted in increased protein aggregation but did not influence cell viability. ..
  40. Shewmaker F, Kerner M, Hayer Hartl M, Klein G, Georgopoulos C, Landry S. A mobile loop order-disorder transition modulates the speed of chaperonin cycling. Protein Sci. 2004;13:2139-48 pubmed
    ..The ordering and binding of GroES co-chaperonin mobile loops accompany an ATP-dependent conformational change in the GroEL chaperonin that promotes ..
  41. Kawata Y, Hongo K, Nosaka K, Furutsu Y, Mizobata T, Nagai J. The role of ATP hydrolysis in the function of the chaperonin GroEL: dynamic complex formation with GroES. FEBS Lett. 1995;369:283-6 pubmed understand the role of ATP hydrolysis of the chaperonin GroEL during protein folding, we have studied GroEL-GroES complex formation in the presence of ATP or ADP by using capillary electrophoresis and surface plasmon resonance...
  42. Chaudhry C, Farr G, Todd M, Rye H, Brunger A, Adams P, et al. Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics. EMBO J. 2003;22:4877-87 pubmed
    ..cis folding by the chaperonin GroEL is triggered by the binding of ATP but not ADP, along with cochaperonin GroES, to the same ring as non-native polypeptide, ejecting polypeptide into an encapsulated hydrophilic chamber...
  43. Koike Takeshita A, Shimamura T, Yokoyama K, Yoshida M, Taguchi H. Leu309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroEL. J Biol Chem. 2006;281:962-7 pubmed
    In the crystal structure of the native GroEL.GroES.substrate protein complex from Thermus thermophilus, one GroEL subunit makes contact with two GroES subunits...
  44. Sewell B, Best R, Chen S, Roseman A, Farr G, Horwich A, et al. A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation. Nat Struct Mol Biol. 2004;11:1128-33 pubmed
    ..Consistent with the loss of negative cooperativity between rings, the cochaperonin GroES binds simultaneously to both E461K rings...
  45. Machida K, Fujiwara R, Tanaka T, Sakane I, Hongo K, Mizobata T, et al. Gly192 at hinge 2 site in the chaperonin GroEL plays a pivotal role in the dynamic apical domain movement that leads to GroES binding and efficient encapsulation of substrate proteins. Biochim Biophys Acta. 2009;1794:1344-54 pubmed publisher
    ..and characterization using surface plasmon resonance analysis, we found that GroEL G192W was capable of binding GroES even in the absence of ATP to form a very stable GroEL-GroES complex, which could not be dissociated even upon ..
  46. Georgopoulos C, Hendrix R, Kaiser A, Wood W. Role of the host cell in bacteriophage morphogenesis: effects of a bacterial mutation on T4 head assembly. Nat New Biol. 1972;239:38-41 pubmed
  47. Sakane I, Hongo K, Motojima F, Murayama S, Mizobata T, Kawata Y. Structural stability of covalently linked GroES heptamer: advantages in the formation of oligomeric structure. J Mol Biol. 2007;367:1171-85 pubmed publisher
    ..association stabilizes oligomeric proteins, a single polypeptide chain variant of heptameric co-chaperonin GroES (tandem GroES) was constructed from Escherichia coli heptameric GroES by linking consecutively the C-terminal of ..
  48. Fredriksson A, Nystrom T. Conditional and replicative senescence in Escherichia coli. Curr Opin Microbiol. 2006;9:612-8 pubmed
    ..Thus, bacterial physiology might entail both conditional and mandatory aging processes. ..
  49. Donald L, Stokell D, Holliday N, Ens W, Standing K, Duckworth H. Multiple equilibria of the Escherichia coli chaperonin GroES revealed by mass spectrometry. Protein Sci. 2005;14:1375-9 pubmed
    ..mass spectrometry has been used to study the assembly of the heptamer of the Escherichia coli cochaperonin protein GroES, a system previously described as a monomer-heptamer equilibrium...
  50. Hemmingsen S, Woolford C, van der Vies S, Tilly K, Dennis D, Georgopoulos C, et al. Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature. 1988;333:330-4 pubmed publisher
    ..Chaperonins comprise a class of molecular chaperones that are found in chloroplasts, mitochondria and prokaryotes. Assisted post-translational assembly of oligomeric protein structures is emerging as a general cellular phenomenon...
  51. Braig K, Adams P, Brunger A. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution. Nat Struct Biol. 1995;2:1083-94 pubmed
    ..The regions of the protein involved in polypeptide and GroES binding show unusually high B factors; these values may indicate mobility or discrete disorder...
  52. Chen D, Song J, Chuang D, Chiu W, Ludtke S. An expanded conformation of single-ring GroEL-GroES complex encapsulates an 86 kDa substrate. Structure. 2006;14:1711-22 pubmed
    Electron cryomicroscopy reveals an unprecedented conformation of the single-ring mutant of GroEL (SR398) bound to GroES in the presence of Mg-ATP...
  53. Song J, Li J, Huang Y, Chuang D. Encapsulation of an 86-kDa assembly intermediate inside the cavities of GroEL and its single-ring variant SR1 by GroES. J Biol Chem. 2003;278:2515-21 pubmed
    ..heterotetramer of human mitochondrial branched-chain alpha-ketoacid dehydrogenase (BCKD), chaperonins GroEL/GroES interact with the kinetically trapped heterodimeric (alphabeta) intermediate to facilitate conversion of the ..
  54. Kandror O, Sherman M, Rhode M, Goldberg A. Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins. EMBO J. 1995;14:6021-7 pubmed
    In Escherichia coli, the molecular chaperones of hsp60/hsp10 (GroEL/GroES) families are required not only for protein folding but also for the rapid degradation of certain abnormal proteins...
  55. Higurashi T, Nosaka K, Mizobata T, Nagai J, Kawata Y. Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model. J Mol Biol. 1999;291:703-13 pubmed
    The guanidine-hydrochloride (Gdn-HCl) induced unfolding and refolding characteristics of the co-chaperonin GroES from Escherichia coli, a homoheptamer of subunit molecular mass 10,000 Da, were studied by using intrinsic fluorescence, 1-..
  56. Cliff M, Limpkin C, Cameron A, Burston S, Clarke A. Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE. J Biol Chem. 2006;281:21266-75 pubmed
    We have identified five structural rearrangements in GroEL induced by the ordered binding of ATP and GroES. The first discernable rearrangement (designated T --> R(1)) is a rapid, cooperative transition that appears not to be ..
  57. Gragerov A, Nudler E, Komissarova N, Gaitanaris G, Gottesman M, Nikiforov V. Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli. Proc Natl Acad Sci U S A. 1992;89:10341-4 pubmed
    ..Overproduction of either GroEL and GroES or DnaK and DnaJ prevents aggregation...
  58. Chow I, Barnett M, Zolkiewski M, Baneyx F. The N-terminal domain of Escherichia coli ClpB enhances chaperone function. FEBS Lett. 2005;579:4242-8 pubmed
    ..Our results are consistent with a model in which the N-domain of ClpB95 maximizes substrate processing under conditions where the cellular supply of free DnaK-DnaJ is limiting. ..
  59. García Fruitós E, Martínez Alonso M, Gonzalez Montalban N, Valli M, Mattanovich D, Villaverde A. Divergent genetic control of protein solubility and conformational quality in Escherichia coli. J Mol Biol. 2007;374:195-205 pubmed
    ..Most of the tested genetic deficiencies in different cytosolic chaperones and proteases (affecting DnaK, GroEL, GroES, ClpB, ClpP and Lon at different extents) resulted in much less soluble but unexpectedly more fluorescent ..
  60. Ying B, Taguchi H, Kondo M, Ueda T. Co-translational involvement of the chaperonin GroEL in the folding of newly translated polypeptides. J Biol Chem. 2005;280:12035-40 pubmed exhibit overlapping co-translational roles, whereas the cage-shaped GroEL, with the aid of the co-chaperonin, GroES, and ATP, is believed to be implicated in folding only after the polypeptides are released from the ribosome...
  61. Kaur Y, Horowitz P. Prodan fluorescence mimics the GroEL folding cycle. Protein J. 2004;23:475-81 pubmed
    ..However prodan bound to GroEL, GroEL-ATP, and GroEL-ATP-GroES shows emission peaks of intensities 500,000, 540,000, and 480,000 cps at 515, 512 and 515 nm, respectively, thus ..
  62. Schlieker C, Tews I, Bukau B, Mogk A. Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides. FEBS Lett. 2004;578:351-6 pubmed
    ..These findings support a ClpB-dependent threading mechanism as an integral part of the disaggregation reaction. ..
  63. Taura T, Kusukawa N, Yura T, Ito K. Transient shut off of Escherichia coli heat shock protein synthesis upon temperature shift down. Biochem Biophys Res Commun. 1989;163:438-43 pubmed
    ..The synthesis of beta-galactosidase directed by transcription initiated at the groE promoter behaved similarly, suggesting that this regulation, termed "reverse heat shock response", occurs at the transcriptional level. ..
  64. Yamamori T, Yura T. Temperature-induced synthesis of specific proteins in Escherichia coli: evidence for transcriptional control. J Bacteriol. 1980;142:843-51 pubmed
    ..Evidence suggests that E. coli cells somehow "recognize" the temperature change and activate transcription of several distinct operons, one of which contains the mop (morphogenesis of phages; groE) gene. ..
  65. Shirai Y, Akiyama Y, Ito K. Suppression of ftsH mutant phenotypes by overproduction of molecular chaperones. J Bacteriol. 1996;178:1141-5 pubmed
    ..The growth retardation was partially suppressed by overproduction of GroEL/GroES (Hsp60/Hsp10) or HtpG (Hsp90), although these chaperones could not totally substitute for FtsH...
  66. Sakane I, Ikeda M, Matsumoto C, Higurashi T, Inoue K, Hongo K, et al. Structural stability of oligomeric chaperonin 10: the role of two beta-strands at the N and C termini in structural stabilization. J Mol Biol. 2004;344:1123-33 pubmed
    Chaperonin 10 (cpn10) is a well-conserved subgroup of the molecular chaperone family. GroES, the cpn10 from Escherichia coli, is composed of seven 10kDa subunits, which form a dome-like oligomeric ring structure...
  67. Erbse A, Dougan D, Bukau B. A folding machine for many but a master of none. Nat Struct Biol. 2003;10:84-6 pubmed
  68. Thomas J, Baneyx F. ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells. Mol Microbiol. 2000;36:1360-70 pubmed
    DnaK-DnaJ-GrpE and GroEL-GroES are the best-characterized molecular chaperone systems in the cytoplasm of Escherichia coli...
  69. Henzel W, Billeci T, Stults J, Wong S, Grimley C, Watanabe C. Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc Natl Acad Sci U S A. 1993;90:5011-5 pubmed
    ..One of the spots contained an N-terminally blocked protein that required enzymatic cleavage, peptide separation, and Edman degradation for confirmation of its identity...
  70. Zeilstra Ryalls J, Fayet O, Georgopoulos C. The universally conserved GroE (Hsp60) chaperonins. Annu Rev Microbiol. 1991;45:301-25 pubmed
  71. Sameshima T, Ueno T, Iizuka R, Ishii N, Terada N, Okabe K, et al. Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle. J Biol Chem. 2008;283:23765-73 pubmed publisher
    ..GroEL assists protein folding with its cochaperonin GroES in an ATP-dependent manner in vitro and in vivo...
  72. Koike Takeshita A, Yoshida M, Taguchi H. Revisiting the GroEL-GroES reaction cycle via the symmetric intermediate implied by novel aspects of the GroEL(D398A) mutant. J Biol Chem. 2008;283:23774-81 pubmed publisher
    The Escherichia coli chaperonin GroEL is a double-ring chaperone that assists in protein folding with the aid of GroES and ATP...
  73. Segal R, Ron E. Regulation and organization of the groE and dnaK operons in Eubacteria. FEMS Microbiol Lett. 1996;138:1-10 pubmed
    ..They contain only the groES and groEL genes and always in the same order...
  74. Vorderwülbecke S, Kramer G, Merz F, Kurz T, Rauch T, Zachmann Brand B, et al. Low temperature of GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor DnaK. FEBS Lett. 2005;579:181-7 pubmed
    ..of deltatigdeltadnaK52 cells is abrogated either by growth below 30 degrees C or by overproduction of GroEL/GroES. At 23 degrees C deltatigdeltadnaK52 cells were viable and showed only minor protein aggregation...
  75. de Marco A. Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli. Nat Protoc. 2007;2:2632-9 pubmed
    ..Applying such a strategy, we could increase the solubility of 70% of the tested constructs with yields of up to 42-fold more protein than in controls. The procedure takes 2 d. ..
  76. Takagi F, Koga N, Takada S. How protein thermodynamics and folding mechanisms are altered by the chaperonin cage: molecular simulations. Proc Natl Acad Sci U S A. 2003;100:11367-72 pubmed
    ..We also show how ensemble of folding pathways are altered by the chaperonin-like cage calculating a variant of value used in the study of spontaneous folding. ..
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    ..protein folding assumes that the substrate protein in the cage, formed by GroEL central cavity capped with GroES, is isolated from outside and exists as a free polypeptide...
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    The GroEL/GroES chaperonin system of Escherichia coli forms a nano-cage allowing single protein molecules to fold in isolation...
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    ..only 84 of the approximately 2400 cytosolic proteins expressed in minimal media depend absolutely on the GroEL/GroES chaperone system to avoid aggregation...
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    ..Functional implications of this distinct localization are discussed in the context of Escherichia coli protein quality control. ..
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    ..The cochaperonin GroES plays a passive role in the R''-->T transition...
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    ..A well-characterized molecular chaperone system is the chaperonin GroEL/GroES from Escherichia coli which has a homolog found in the eukaryotic cytosol called CCT...
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    ..apical domain conformers to bind co-chaperone and substrate, model peptides corresponding to the mobile loop of GroES and to helix D from rhodanese were studied...
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    ..The chaperonin, GroEL, is an essential molecular chaperone that mediates protein folding together with its cofactor, GroES, in Escherichia coli...
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    ..Our data indicate a general role for the groE operon products, the GroEL and GroES proteins, in the folding-assembly pathways of many proteins.
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    ..g. TIM barrel proteins that need GroE for folding versus TIM barrels that fold independently) be used more extensively in such studies. ..