groL

Summary

Gene Symbol: groL
Description: Cpn60 chaperonin GroEL, large subunit of GroESL
Alias: ECK4137, JW4103, groEL, mopA
Species: Escherichia coli str. K-12 substr. MG1655
Products:     groL

Top Publications

  1. 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 crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally symmetrical rings stacked back-to-back with dyad symmetry...
  2. Fenton W, Kashi Y, Furtak K, Horwich A. Residues in chaperonin GroEL required for polypeptide binding and release. Nature. 1994;371:614-9 pubmed publisher
    ..To gain further insight into the mechanism of polypeptide binding and release by the chaperonin GroEL from Escherichia coli, we have undertaken a mutational analysis that relates the functional properties of GroEL to ..
  3. 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)..
  4. Wang J, Herman C, Tipton K, Gross C, Weissman J. Directed evolution of substrate-optimized GroEL/S chaperonins. Cell. 2002;111:1027-39 pubmed
    b>GroEL/S chaperonin ring complexes fold many unrelated proteins...
  5. 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...
  6. Machida K, Kono Okada A, Hongo K, Mizobata T, Kawata Y. Hydrophilic residues 526 KNDAAD 531 in the flexible C-terminal region of the chaperonin GroEL are critical for substrate protein folding within the central cavity. J Biol Chem. 2008;283:6886-96 pubmed publisher
    The final 23 residues in the C-terminal region of Escherichia coli GroEL are invisible in crystallographic analyses due to high flexibility...
  7. Tang Y, Chang H, Chakraborty K, Hartl F, Hayer Hartl M. Essential role of the chaperonin folding compartment in vivo. EMBO J. 2008;27:1458-68 pubmed publisher
    The GroEL/GroES chaperonin system of Escherichia coli forms a nano-cage allowing single protein molecules to fold in isolation...
  8. Kusukawa N, Yura T, Ueguchi C, Akiyama Y, Ito K. Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli. EMBO J. 1989;8:3517-21 pubmed
    Escherichia coli heat-shock proteins GroES and GroEL are essential cytoplasmic proteins, which have been termed 'chaperonins' because of their ability to assist protein assembly of bacteriophage capsids and multimeric enzymes of foreign ..
  9. Lund P. Multiple chaperonins in bacteria--why so many?. FEMS Microbiol Rev. 2009;33:785-800 pubmed publisher
    ..The mechanism of action of the Escherichia coli GroEL protein has been studied in great detail...

More Information

Publications106 found, 100 shown here

  1. Mizobata T, Akiyama Y, Ito K, Yumoto N, Kawata Y. Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. Refolding is enhanced in the presence of ADP. J Biol Chem. 1992;267:17773-9 pubmed
    ..The GroEL subunit was required for this improvement in refolding yield, whereas the GroES subunit was not...
  2. Braig K, Simon M, Furuya F, Hainfeld J, Horwich A. A polypeptide bound by the chaperonin groEL is localized within a central cavity. Proc Natl Acad Sci U S A. 1993;90:3978-82 pubmed
    ..0 nm in diameter. We sought to identify the site on the Escherichia coli chaperonin groEL, where the "molten globule"-like intermediate of dihydrofolate reductase (DHFR) becomes bound, by ..
  3. Taguchi H. Chaperonin GroEL meets the substrate protein as a "load" of the rings. J Biochem. 2005;137:543-9 pubmed
    Chaperonin GroEL is an essential molecular chaperone that assists protein folding in the cell...
  4. Sherman MYu -, Goldberg A. Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation. Nature. 1992;357:167-9 pubmed
    ..Certain heat-shock proteins such as groEL, called 'chaperonins', can prevent misfolding and promote the refolding and proper assembly of unfolded ..
  5. Kawata Y, Nosaka K, Hongo K, Mizobata T, Nagai J. Chaperonin GroE and ADP facilitate the folding of various proteins and protect against heat inactivation. FEBS Lett. 1994;345:229-32 pubmed
    In the presence of ADP, the molecular chaperones GroEL and GroES from Escherichia coli not only facilitated the refolding of various proteins, but also prevented their irreversible heat inactivation in vitro...
  6. Melkani G, Zardeneta G, Mendoza J. The ATPase activity of GroEL is supported at high temperatures by divalent cations that stabilize its structure. Biometals. 2003;16:479-84 pubmed
    Previously, we reported that the ATPase activity of GroEL that requires potassium and magnesium was highly temperature dependent in the 25-60 degrees C range...
  7. van Duijn E, Bakkes P, Heeren R, van den Heuvel R, van Heerikhuizen H, van der Vies S, et al. Monitoring macromolecular complexes involved in the chaperonin-assisted protein folding cycle by mass spectrometry. Nat Methods. 2005;2:371-6 pubmed publisher
    ..We found that GroEL can bind up to two unfolded gp23 substrate molecules...
  8. Carrió M, Villaverde A. Localization of chaperones DnaK and GroEL in bacterial inclusion bodies. J Bacteriol. 2005;187:3599-601 pubmed
    By immunostaining and transmission electron microscopy, chaperones DnaK and GroEL have been identified at the solvent-exposed surface of bacterial inclusion bodies and entrapped within these aggregates, respectively...
  9. Horst R, Bertelsen E, Fiaux J, Wider G, Horwich A, Wuthrich K. Direct NMR observation of a substrate protein bound to the chaperonin GroEL. Proc Natl Acad Sci U S A. 2005;102:12748-53 pubmed
    The reaction cycle and the major structural states of the molecular chaperone GroEL and its cochaperone, GroES, are well characterized...
  10. Wolf S. Single-ring GroEL: an expanded view. Structure. 2006;14:1599-600 pubmed
  11. Goyal K, Qamra R, Mande S. Multiple gene duplication and rapid evolution in the groEL gene: functional implications. J Mol Evol. 2006;63:781-7 pubmed
    The chaperonins, GroEL and GroES, are present ubiquitously and provide a paradigm in the understanding of assisted protein folding. Due to its essentiality of function, GroEL exhibits high sequence conservation across species...
  12. De Carlo S, Boisset N, Hoenger A. High-resolution single-particle 3D analysis on GroEL prepared by cryo-negative staining. Micron. 2008;39:934-43 pubmed
    ..Using the well known E. coli GroEL chaperonin, we could show that the structure is well preserved to approximately 10 A resolution...
  13. Sohlberg B, Lundberg U, Hartl F, von Gabain A. Functional interaction of heat shock protein GroEL with an RNase E-like activity in Escherichia coli. Proc Natl Acad Sci U S A. 1993;90:277-81 pubmed
    ..mutation of the ams/rne gene that seems to be complemented at nonpermissive temperatures by a fragment of the groEL gene...
  14. Wang Q, Buckle A, Fersht A. Stabilization of GroEL minichaperones by core and surface mutations. J Mol Biol. 2000;298:917-26 pubmed
    We report the crystal structures of two hexa-substituted mutants of a GroEL minichaperone that are more stable than wild-type by 7.0 and 6.1 kcal mol(-1)...
  15. Ferrer M, Chernikova T, Yakimov M, Golyshin P, Timmis K. Chaperonins govern growth of Escherichia coli at low temperatures. Nat Biotechnol. 2003;21:1266-7 pubmed
  16. 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. ..
  17. 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
    ..lethality 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...
  18. Depping R, Lohaus C, Meyer H, Rüger W. The mono-ADP-ribosyltransferases Alt and ModB of bacteriophage T4: target proteins identified. Biochem Biophys Res Commun. 2005;335:1217-23 pubmed
    ..E. coli trigger factor and the elongation factor EF-Tu were 2 targets of ModB action, and these proteins were among the 10 identified as targets of Alt, hinting that these factors are involved in phage replication. ..
  19. Krishna K, Rao G, Rao K. Chaperonin GroEL: structure and reaction cycle. Curr Protein Pept Sci. 2007;8:418-25 pubmed
    The structure of Escherichia coli chaperonin GroEL was studied using various experimental tools. Such studies produced information about its structure with increasing details...
  20. 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
    The subunit structure of chaperonin GroEL is divided into three domains; the apical domain, the intermediate domain, and the equatorial domain. Each domain has a specific role in the chaperonin mechanism...
  21. Walter S, Lorimer G, Schmid F. A thermodynamic coupling mechanism for GroEL-mediated unfolding. Proc Natl Acad Sci U S A. 1996;93:9425-30 pubmed
    ..It was suggested that GroEL, the chaperonin of Escherichia coli, exerts this function 1 unfolding such intermediates, presumably in a ..
  22. Horowitz P, Lorimer G, Ybarra J. GroES in the asymmetric GroEL14-GroES7 complex exchanges via an associative mechanism. Proc Natl Acad Sci U S A. 1999;96:2682-6 pubmed
    ..These results explain how the GroEL14 cavity can become reversibly accessible to proteins under in vivo conditions that favor 2:1 complexes. ..
  23. Wertz J, Goldstone C, Gordon D, Riley M. A molecular phylogeny of enteric bacteria and implications for a bacterial species concept. J Evol Biol. 2003;16:1236-48 pubmed
    ..Sequences from five housekeeping genes (gapA, groEL, gyrA, ompA, and pgi) and the 16S rRNA gene were used to infer individual gene trees and were concatenated to ..
  24. Panda M, Horowitz P. Activation parameters for the spontaneous and pressure-induced phases of the dissociation of single-ring GroEL (SR1) chaperonin. Protein J. 2004;23:85-94 pubmed
    We investigated the dissociation of single-ring heptameric GroEL (SR1) by high hydrostatic pressure in the range 0.5-3.0 kbar. The kinetics were studied as a function of temperature in the range 15-35 degrees C...
  25. Rosen R, Becher D, Büttner K, Biran D, Hecker M, Ron E. Highly phosphorylated bacterial proteins. Proteomics. 2004;4:3068-77 pubmed
    ..Therefore, it is possible that the highly phosphorylated proteins represent a group of proteins tagged for degradation by phosphorylation. Such a tagging process may be involved in a general bacterial degradation pathway. ..
  26. Zhao W, Yao S, Hsing I. A microsystem compatible strategy for viable Escherichia coli detection. Biosens Bioelectron. 2006;21:1163-70 pubmed
    ..e. mRNAs of a common E. coli GroEL heat shock protein (hsp)...
  27. Yoshimi T, Hongo K, Mizobata T, Kawata Y. Multiple structural transitions of the GroEL subunit are sensitive to intermolecular interactions with cochaperonin and refolding polypeptide. J Biochem. 2006;139:407-19 pubmed
    ..determine the specific roles of the numerous conformational changes that are observed in the bacterial chaperonin GroEL, by performing stopped-flow experiments on GroEL R231W in the presence of a refolding substrate protein...
  28. 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...
  29. Kiser P, Lodowski D, Palczewski K. Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007;63:457-61 pubmed
    b>GroEL is a member of the ATP-dependent chaperonin family that promotes the proper folding of many cytosolic bacterial proteins...
  30. 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...
  31. Siegers K, Waldmann T, Leroux M, Grein K, Shevchenko A, Schiebel E, et al. Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J. 1999;18:75-84 pubmed
    ..This compartment sequesters newly synthesized actin and other aggregation-sensitive polypeptides from the crowded macromolecular environment of the cytosol, thereby allowing their efficient folding. ..
  32. Mukherjee K, Nagai H, Shimamoto N, Chatterji D. GroEL is involved in activation of Escherichia coli RNA polymerase devoid of the omega subunit in vivo. Eur J Biochem. 1999;266:228-35 pubmed
    ..The omega-less RNA polymerase from omega-less strains recruits the chaperonin, GroEL (unlike the wild-type enzyme), suggesting a structural deformity of the mutant enzyme...
  33. Fiaux J, Bertelsen E, Horwich A, Wuthrich K. NMR analysis of a 900K GroEL GroES complex. Nature. 2002;418:207-11 pubmed
    ..co-chaperonin GroES (M(r) 72K), either free in solution or in complex with the homotetradecameric chaperonin GroEL (M(r) 800K) or with the single-ring GroEL variant SR1 (M(r) 400K)...
  34. 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 ..
  35. Layton J, Foster P. Error-prone DNA polymerase IV is regulated by the heat shock chaperone GroE in Escherichia coli. J Bacteriol. 2005;187:449-57 pubmed
    ..The groE operon consists of two genes, groES and groEL; point mutations in either gene conferred the same phenotype, reducing Lac+ adaptive mutation 10- to 20-fold...
  36. 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...
  37. Chapman E, Farr G, Usaite R, Furtak K, Fenton W, Chaudhuri T, et al. Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL. Proc Natl Acad Sci U S A. 2006;103:15800-5 pubmed
    In a newly isolated temperature-sensitive lethal Escherichia coli mutant affecting the chaperonin GroEL, we observed wholesale aggregation of newly translated proteins...
  38. Liu H, Kovacs E, Lund P. Characterisation of mutations in GroES that allow GroEL to function as a single ring. FEBS Lett. 2009;583:2365-71 pubmed publisher
    The chaperonin GroEL contains two seven-subunit rings, and allosteric signals between them are required to complete the GroEL reaction cycle...
  39. Wang Q, Buckle A, Foster N, Johnson C, Fersht A. Design of highly stable functional GroEL minichaperones. Protein Sci. 1999;8:2186-93 pubmed
    b>GroEL minichaperones have potential in the biotechnology industry for the refolding of recombinant proteins...
  40. Mizobata T, Kawata Y. [Dynamic conformational changes which support the function of molecular chaperone GroE]. Seikagaku. 2001;73:361-6 pubmed
  41. Petersson L, Carrió M, Vera A, Villaverde A. The impact of dnaKJ overexpression on recombinant protein solubility results from antagonistic effects on the control of protein quality. Biotechnol Lett. 2004;26:595-601 pubmed
    ..of VP1LAC is progressively enhanced, the heat-shock response is down-regulated as revealed by decreasing levels of GroEL. This is accompanied by an increasing yield of VP1LAC and a non-regular evolution of its insoluble fraction, at ..
  42. Georgopoulos C. Toothpicks, serendipity and the emergence of the Escherichia coli DnaK (Hsp70) and GroEL (Hsp60) chaperone machines. Genetics. 2006;174:1699-707 pubmed
  43. Jacob E, Horovitz A, Unger R. Different mechanistic requirements for prokaryotic and eukaryotic chaperonins: a lattice study. Bioinformatics. 2007;23:i240-8 pubmed
    ..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...
  44. Chen J, Yagi H, Sormanni P, Vendruscolo M, Makabe K, Nakamura T, et al. Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperone. FEBS Lett. 2012;586:1120-7 pubmed publisher
    The chaperonin GroEL plays an essential role in promoting protein folding and in protecting against misfolding and aggregation in the cellular environment...
  45. Donnelly C, Walker G. Coexpression of UmuD' with UmuC suppresses the UV mutagenesis deficiency of groE mutants. J Bacteriol. 1992;174:3133-9 pubmed
    ..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.
  46. Chanda P, Ono M, Kuwano M, Kung H. Cloning, sequence analysis, and expression of alteration of the mRNA stability gene (ams+) of Escherichia coli. J Bacteriol. 1985;161:446-9 pubmed
    ..We discussed the possible role(s) of the ams+ gene product in affecting mRNA stability. ..
  47. Chen L, Sigler P. The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity. Cell. 1999;99:757-68 pubmed
    The chaperonin GroEL is a double toriodal assembly that with its cochaperonin GroES facilitates protein folding with an ATP-dependent mechanism...
  48. Jones H, Preuss M, Wright M, Miller A. The mechanism of GroEL/GroES folding/refolding of protein substrates revisited. Org Biomol Chem. 2006;4:1223-35 pubmed
    ..thermodynamics and kinetics of zinc-cytochrome c (ZnCyt c) interactions with Escherichia coli molecular chaperone GroEL (Chaperonin 60; Cpn60) are described...
  49. de Gier J, Luirink J. Biogenesis of inner membrane proteins in Escherichia coli. Mol Microbiol. 2001;40:314-22 pubmed
    ..Here, we review and discuss recent advances in our understanding of the biogenesis of inner membrane proteins in E. coli. ..
  50. 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
    b>GroEL C138W is a mutant 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...
  51. Horikoshi M, Yura T, Tsuchimoto S, Fukumori Y, Kanemori M. Conserved region 2.1 of Escherichia coli heat shock transcription factor sigma32 is required for modulating both metabolic stability and transcriptional activity. J Bacteriol. 2004;186:7474-80 pubmed
    ..Besides greater stability, the levels of heat shock proteins, such as DnaK and GroEL, increased in cells producing stable sigma32...
  52. Hyeon C, Lorimer G, Thirumalai D. Dynamics of allosteric transitions in GroEL. Proc Natl Acad Sci U S A. 2006;103:18939-44 pubmed
    The chaperonin GroEL-GroES, a machine that helps proteins to fold, cycles through a number of allosteric states, the T state, with high affinity for substrate proteins, the ATP-bound R state, and the R" (GroEL-ADP-GroES) complex...
  53. Paul S, Singh C, Mishra S, Chaudhuri T. The 69 kDa Escherichia coli maltodextrin glucosidase does not get encapsulated underneath GroES and folds through trans mechanism during GroEL/GroES-assisted folding. FASEB J. 2007;21:2874-85 pubmed
    Escherichia coli chaperonin GroEL and GroES assist in folding of a wide variety of substrate proteins in the molecular mass range of approximately 50 kDa, using cis mechanism, but limited information is available on how they assist in ..
  54. 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
    The GroEL/ES chaperonin system is required for the assisted folding of many proteins. How these substrate proteins are encapsulated within the GroEL-GroES cavity is poorly understood...
  55. Timms A, Bridges B. Reversion of the tyrosine ochre strain Escherichia coli WU3610 under starvation conditions depends on a new gene tas. Genetics. 1998;148:1627-35 pubmed
    ..The target gene for mutation is not tas, although an increase in the expression of this gene, for example, resulting from a suppressor mutation affecting supercoiling, could be responsible for the slow-growing Tyr+ phenotype. ..
  56. Yamaguchi Y, Tomoyasu T, Takaya A, Morioka M, Yamamoto T. Effects of disruption of heat shock genes on susceptibility of Escherichia coli to fluoroquinolones. BMC Microbiol. 2003;3:16 pubmed
    ..Mutations in dnaK, groEL, and lon increased this susceptibility; the lon mutant exhibited the greatest effects...
  57. Ranford J, Coates A, Henderson B. Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones. Expert Rev Mol Med. 2000;2:1-17 pubmed
    The chaperonins are a subgroup of oligomeric molecular chaperones; the best-studied examples are chaperonin 60 (GroEL) and chaperonin 10 (GroES), both from the bacterium Escherichia coli...
  58. 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
    b>GroEL and DnaK with their cofactors constitute the major chaperone systems promoting protein folding in the Escherichia coli cytosol...
  59. Bhutani N, Udgaonkar J. GroEL channels the folding of thioredoxin along one kinetic route. J Mol Biol. 2001;314:1167-79 pubmed
    ..The small protein thioredoxin from Escherichia coli is one such protein. The effect of the chaperonin GroEL on modulating the complex energy landscape that separates the unfolded ensemble from the native state of ..
  60. Tokuriki N, Tawfik D. Chaperonin overexpression promotes genetic variation and enzyme evolution. Nature. 2009;459:668-73 pubmed publisher
    ..We examined the ability of the Escherichia coli GroEL/GroES chaperonins to buffer destabilizing and adaptive mutations...
  61. Miki T, Orita T, Furuno M, Horiuchi T. Control of cell division by sex factor F in Escherichia coli. III. Participation of the groES (mopB) gene of the host bacteria. J Mol Biol. 1988;201:327-38 pubmed
    ..These observations suggest to us that the morphogenesis gene groES plays a key role in coupling between replication of the F plasmid and cell division of the host cells. ..
  62. Llorca O, Carrascosa J, Valpuesta J. Biochemical characterization of symmetric GroEL-GroES complexes. Evidence for a role in protein folding. J Biol Chem. 1996;271:68-76 pubmed
    When chaperonins GroEL and GroES are incubated under functional conditions in the presence of ATP (5 mM) and K+ (150 mM), GroEL-GroES complexes appear in the incubation mixture, that are either asymmetric (1:1 GroEL:GroES oligomer ratio) ..
  63. Chaudhry C, Horwich A, Brunger A, Adams P. Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states. J Mol Biol. 2004;342:229-45 pubmed
    Large rigid-body domain movements are critical to GroEL-mediated protein folding, especially apical domain elevation and twist associated with the formation of a folding chamber upon binding ATP and co-chaperonin GroES...
  64. 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. ..
  65. Zheng W, Brooks B, Thirumalai D. Allosteric transitions in the chaperonin GroEL are captured by a dominant normal mode that is most robust to sequence variations. Biophys J. 2007;93:2289-99 pubmed
    The Escherichia coli chaperonin GroEL, which helps proteins to fold, consists of two heptameric rings stacked back-to-back...
  66. 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...
  67. 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
    Binding and folding of substrate proteins by the molecular chaperone GroEL alternates between its two seven-membered rings in an ATP-regulated manner...
  68. 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. ..
  69. 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
    ..Here we focus on the roles of other HSPs (heat-shock proteins), including the chaperonin GroEL, in addition to DnaK, in ribosome biogenesis at high temperature...
  70. Guisbert E, Herman C, Lu C, Gross C. A chaperone network controls the heat shock response in E. coli. Genes Dev. 2004;18:2812-21 pubmed
    ..coli to regulate sigma32, and we demonstrate that the GroEL/S chaperonin is an additional regulator of sigma32...
  71. Gupta P, Aggarwal N, Batra P, Mishra S, Chaudhuri T. Co-expression of chaperonin GroEL/GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth characteristics of Escherichia coli. Int J Biochem Cell Biol. 2006;38:1975-85 pubmed
    Over last two decades many researchers have demonstrated the mechanisms of how the Escherichia coli chaperonin GroEL and GroES work in the binding and folding of different aggregation prone substrate proteins both in vivo and in vitro...
  72. Masters M, Blakely G, Coulson A, McLennan N, Yerko V, Acord J. Protein folding in Escherichia coli: the chaperonin GroE and its substrates. Res Microbiol. 2009;160:267-77 pubmed publisher
    ..We consider its obligate substrates, the 8 that are both obligate and essential, and the prospects for constructing a mutant that could survive without it. Structural features of GroE-dependent polypeptides are also considered. ..
  73. Billerbeck S, Calles B, Müller C, De Lorenzo V, Panke S. Towards functional orthogonalisation of protein complexes: individualisation of GroEL monomers leads to distinct quasihomogeneous single rings. Chembiochem. 2013;14:2310-21 pubmed publisher
    The essential molecular chaperonin GroEL is an example of a functionally highly versatile cellular machine with a wide variety of in vitro applications ranging from protein folding to drug release...
  74. Kusukawa N, Yura T. Heat shock protein GroE of Escherichia coli: key protective roles against thermal stress. Genes Dev. 1988;2:874-82 pubmed
    ..in the groE upstream region, resulting in high-level synthesis of major heat shock proteins GroE (GroES and GroEL)...
  75. Maguire M, Coates A, Henderson B. Chaperonin 60 unfolds its secrets of cellular communication. Cell Stress Chaperones. 2002;7:317-29 pubmed
    ..The structure of the most widely studied Cpn60, Escherichia coli GroEL, has been solved and its mechanism of protein folding action largely established...
  76. Fiaux J, Bertelsen E, Horwich A, Wuthrich K. Uniform and residue-specific 15N-labeling of proteins on a highly deuterated background. J Biomol NMR. 2004;29:289-97 pubmed
  77. Parent K, Teschke C. GroEL/S substrate specificity based on substrate unfolding propensity. Cell Stress Chaperones. 2007;12:20-32 pubmed
    Phage P22 wild-type (WT) coat protein does not require GroEL/S to fold but temperature-sensitive-folding (tsf) coat proteins need the chaperone complex for correct folding...
  78. Otsuka Y, Koga M, Iwamoto A, Yonesaki T. A role of RnlA in the RNase LS activity from Escherichia coli. Genes Genet Syst. 2007;82:291-9 pubmed
    ..Among these, triose phosphate isomerase exhibited a remarkable affinity to RnlA. These results suggest that RnlA plays a central role in RNase LS activity and that its activity is regulated by multiple components...
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    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...
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    ..At each of the specified base pairs, substitutions were found which reduced promoter activity by greater than 75%. Activity was also dependent upon the number of base pairs separating the two regions. ..
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    ..Separate overproduction of the major chaperone systems, DnaK/DnaJ and GroEL/GroES, established that the former of these is more important in counteracting protein carbonylation...