chaperonin 10


Summary: A group I chaperonin protein that forms a lid-like structure which encloses the non-polar cavity of the chaperonin complex. The protein was originally studied in BACTERIA where it is commonly referred to as GroES protein.

Top Publications

  1. Kim M, Jernigan R, Chirikjian G. Rigid-cluster models of conformational transitions in macromolecular machines and assemblies. Biophys J. 2005;89:43-55 pubmed
    ..The computational cost of the interpolation no longer scales heavily with the size of structures; instead, it depends strongly on the minimal number of rigid clusters into which the system can be decomposed. ..
  2. Richardson A, Schwager F, Landry S, Georgopoulos C. The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coli. J Biol Chem. 2001;276:4981-7 pubmed
    ..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. ..
  3. Lin K, Lin B, Lian I, Mestril R, Scheffler I, Dillmann W. Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation. Circulation. 2001;103:1787-92 pubmed
  4. Thirumalai D, Lorimer G. Chaperonin-mediated protein folding. Annu Rev Biophys Biomol Struct. 2001;30:245-69 pubmed
    ..Further refinement of this framework may be necessary because single molecule experiments indicate that there is a great dispersion in the time scales governing the dynamics of the chaperonin cycle. ..
  5. Akyol S, Gercel Taylor C, Reynolds L, Taylor D. HSP-10 in ovarian cancer: expression and suppression of T-cell signaling. Gynecol Oncol. 2006;101:481-6 pubmed
    ..Our findings indicate that, as in pregnancy, production and release of HSP10 may be a critical factor in the suppression of T-cell activation, allowing the tumor to escape immune surveillance. ..
  6. 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
    ..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. ..
  7. Rodolico V, Tomasello G, Zerilli M, Martorana A, Pitruzzella A, Gammazza A, et al. Hsp60 and Hsp10 increase in colon mucosa of Crohn’s disease and ulcerative colitis. Cell Stress Chaperones. 2010;15:877-84 pubmed publisher
  8. Kass I, Horovitz A. Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations. Proteins. 2002;48:611-7 pubmed
    ..The results are discussed in the context of available structural, genetic, and biochemical data concerning short- and long-range interactions in the GroE system. ..
  9. Czarnecka A, Campanella C, Zummo G, Cappello F. Heat shock protein 10 and signal transduction: a "capsula eburnea" of carcinogenesis?. Cell Stress Chaperones. 2006;11:287-94 pubmed
    ..In this review, we revise the involvement of Hsp10 in signal transduction pathways and its possible role in cancer etiology. ..

More Information


  1. Bahar I, Rader A. Coarse-grained normal mode analysis in structural biology. Curr Opin Struct Biol. 2005;15:586-92 pubmed
    ..Such applications have provided great insight into the underlying principles linking protein structures to their dynamics and their dynamics to their functions. ..
  2. Ellis R. Protein folding: inside the cage. Nature. 2006;442:360-2 pubmed
  3. Bonshtien A, Weiss C, Vitlin A, Niv A, Lorimer G, Azem A. Significance of the N-terminal domain for the function of chloroplast cpn20 chaperonin. J Biol Chem. 2007;282:4463-9 pubmed
    ..Moreover, only N-cpn20 is necessary for activity of cpn20. However, full and efficient functioning requires both domains. ..
  4. Iwasa H, Meshitsuka S, Hongo K, Mizobata T, Kawata Y. Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: insight into intrinsically disordered proteins. J Biol Chem. 2011;286:21796-805 pubmed publisher
    ..The finding provides a novel insight into the structural process of amyloid fibril formation from a disordered state, which may be applicable to intrinsically disordered proteins in general. ..
  5. Agrawal T, Vats V, Salhan S, Mittal A. Mucosal and peripheral immune responses to chlamydial heat shock proteins in women infected with Chlamydia trachomatis. Clin Exp Immunol. 2007;148:461-8 pubmed
  6. Hansen J, Durr A, Cournu Rebeix I, Georgopoulos C, Ang D, Nielsen M, et al. Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. Am J Hum Genet. 2002;70:1328-32 pubmed
    ..Taken together, our data strongly indicate that the V72I variation is the first disease-causing mutation that has been identified in HSP60...
  7. Horst R, Fenton W, Englander S, Wuthrich K, Horwich A. Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution. Proc Natl Acad Sci U S A. 2007;104:20788-92 pubmed
  8. 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. ..
  9. 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
    ..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. ..
  10. Ranson N, Clare D, Farr G, Houldershaw D, Horwich A, Saibil H. Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes. Nat Struct Mol Biol. 2006;13:147-52 pubmed
  11. 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
    ..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. ..
  12. Corrao S, Campanella C, Anzalone R, Farina F, Zummo G, Conway de Macario E, et al. Human Hsp10 and Early Pregnancy Factor (EPF) and their relationship and involvement in cancer and immunity: current knowledge and perspectives. Life Sci. 2010;86:145-52 pubmed publisher
    ..In this article, we present an overview of various aspects of Hsp10 and EPF as they participate in physiological and pathological processes such as the antitumor response and autoimmune diseases. ..
  13. Sharkia R, Bonshtien A, Mizrahi I, Weiss C, Niv A, Lustig A, et al. On the oligomeric state of chloroplast chaperonin 10 and chaperonin 20. Biochim Biophys Acta. 2003;1651:76-84 pubmed
    ..and mitochondria contain chaperonin systems comprised of homo-oligomeric chaperonin 60 tetradecamers and co-chaperonin 10 heptamers...
  14. 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
    ..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. ..
  15. Guidry J, Wittung Stafshede P. Low stability for monomeric human chaperonin protein 10: interprotein interactions contribute majority of oligomer stability. Arch Biochem Biophys. 2002;405:280-2 pubmed
  16. Lin Z, Rye H. Expansion and compression of a protein folding intermediate by GroEL. Mol Cell. 2004;16:23-34 pubmed
  17. Cappello F, Tripodo C, Farina F, Franco V, Zummo G. HSP10 selective preference for myeloid and megakaryocytic precursors in normal human bone marrow. Eur J Histochem. 2004;48:261-5 pubmed
    ..The present data emphasize the role of HSP10 during cellular homeostasis and encourage further investigations in this field. ..
  18. Keskin O, Bahar I, Flatow D, Covell D, Jernigan R. Molecular mechanisms of chaperonin GroEL-GroES function. Biochemistry. 2002;41:491-501 pubmed
    ..These modes of motion could be used to manipulate the substrate's conformations. ..
  19. Coluzza I, van der Vies S, Frenkel D. Translocation boost protein-folding efficiency of double-barreled chaperonins. Biophys J. 2006;90:3375-81 pubmed
    ..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. ..
  20. Horwich A, Fenton W, Chapman E, Farr G. Two families of chaperonin: physiology and mechanism. Annu Rev Cell Dev Biol. 2007;23:115-45 pubmed
    ..What are the determinants for substrate binding by the type II chaperonins? And is the encapsulated chaperonin cavity a passive container that prevents aggregation, or could it be playing an active role in polypeptide folding? ..
  21. Hu Y, Henderson B, Lund P, Tormay P, Ahmed M, Gurcha S, et al. A Mycobacterium tuberculosis mutant lacking the groEL homologue cpn60.1 is viable but fails to induce an inflammatory response in animal models of infection. Infect Immun. 2008;76:1535-46 pubmed publisher
    ..Cell wall lipid acid composition was not altered in the mutant strain. Thus, it appears that Cpn60.1 is an important agent in the regulation of the cytokine-dependent granulomatous response in M. tuberculosis infection. ..
  22. Clare D, Bakkes P, van Heerikhuizen H, van der Vies S, Saibil H. Chaperonin complex with a newly folded protein encapsulated in the folding chamber. Nature. 2009;457:107-10 pubmed publisher
  23. Cappello F, Rappa F, David S, Anzalone R, Zummo G. Immunohistochemical evaluation of PCNA, p53, HSP60, HSP10 and MUC-2 presence and expression in prostate carcinogenesis. Anticancer Res. 2003;23:1325-31 pubmed
    ..We suggest the further examination, by molecular and genetic studies, of the role of HSP60 and HSP10 during carcinogenesis of the prostate as well as of other organs. ..
  24. Chennubhotla C, Bahar I. Markov propagation of allosteric effects in biomolecular systems: application to GroEL-GroES. Mol Syst Biol. 2006;2:36 pubmed
    ..Comparison with collective modes deduced from normal mode analysis reveals the propensity of global hinge regions to act as messengers in the transmission of allosteric signals. ..
  25. Tang Y, Chang H, Roeben A, Wischnewski D, Wischnewski N, Kerner M, et al. Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Cell. 2006;125:903-14 pubmed
    ..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. ..
  26. Williams B, Vanags D, Hall S, McCormack C, Foley P, Weiss J, et al. Efficacy and safety of chaperonin 10 in patients with moderate to severe plaque psoriasis: evidence of utility beyond a single indication. Arch Dermatol. 2008;144:683-5 pubmed publisher
  27. 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
  28. Pomara G, Cappello F. RE: Heat shock proteins: their role in urological tumors. J Urol. 2003;170:927-8 pubmed
  29. Cappello F, Bellafiore M, David S, Anzalone R, Zummo G. Ten kilodalton heat shock protein (HSP10) is overexpressed during carcinogenesis of large bowel and uterine exocervix. Cancer Lett. 2003;196:35-41 pubmed
    ..These results could stimulate further studies on the pathogenetic role of these proteins during the carcinogenesis as well as their use as diagnostic and prognostic tools in oncology. ..
  30. Kawata Y, Kawagoe M, Hongo K, Miyazaki T, Higurashi T, Mizobata T, et al. Functional communications between the apical and equatorial domains of GroEL through the intermediate domain. Biochemistry. 1999;38:15731-40 pubmed
    ..These results point to a multitude of signals which govern the overall chaperonin mechanism. ..
  31. Keppel F, Rychner M, Georgopoulos C. Bacteriophage-encoded cochaperonins can substitute for Escherichia coli's essential GroES protein. EMBO Rep. 2002;3:893-8 pubmed
    ..Thus, it appears that, despite very little sequence identity with groES, the bacteriophage-encoded Gp31 and CocO proteins are capable of replacing GroES in the folding of E. coli's essential, housekeeping proteins. ..
  32. Kanno R, Koike Takeshita A, Yokoyama K, Taguchi H, Mitsuoka K. Cryo-EM structure of the native GroEL-GroES complex from thermus thermophilus encapsulating substrate inside the cavity. Structure. 2009;17:287-93 pubmed publisher
  33. Higgins D, Hemsley S, Canfield P. Association of uterine and salpingeal fibrosis with chlamydial hsp60 and hsp10 antigen-specific antibodies in Chlamydia-infected koalas. Clin Diagn Lab Immunol. 2005;12:632-9 pubmed
  34. 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
    ..A major advantage of native mass spectrometry is that, given sufficient resolution, it allows the analysis at the picomole level of sensitivity of heterogeneous protein complexes with molecular masses up to several million daltons...
  35. Hartl F, Hayer Hartl M. Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol. 2009;16:574-81 pubmed publisher
  36. 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
    ..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. ..
  37. Farr G, Fenton W, Chaudhuri T, Clare D, Saibil H, Horwich A. Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes. EMBO J. 2003;22:3220-30 pubmed
    ..We conclude that a trans mechanism, involving rounds of binding to an open ring and direct release into the bulk solution, can be generally productive although, where size permits, cis encapsulation supports more efficient folding. ..
  38. Levy Rimler G, Viitanen P, Weiss C, Sharkia R, Greenberg A, Niv A, et al. The effect of nucleotides and mitochondrial chaperonin 10 on the structure and chaperone activity of mitochondrial chaperonin 60. Eur J Biochem. 2001;268:3465-72 pubmed
    ..We propose that the cis (mt-cpn60)14.nucleotide.(mt-cpn10)7 complex is not a stable species and does not bind ADP effectively at its trans binding site. ..
  39. Grason J, Gresham J, Widjaja L, Wehri S, Lorimer G. Setting the chaperonin timer: the effects of K+ and substrate protein on ATP hydrolysis. Proc Natl Acad Sci U S A. 2008;105:17334-8 pubmed publisher
    ..The hydrolysis of ATP by the cis ring constitutes a second, nonvariable timer of the chaperonin cycle. ..
  40. Christensen J, Nielsen M, Hansen J, Füchtbauer A, Füchtbauer E, West M, et al. Inactivation of the hereditary spastic paraplegia-associated Hspd1 gene encoding the Hsp60 chaperone results in early embryonic lethality in mice. Cell Stress Chaperones. 2010;15:851-63 pubmed publisher
    ..Our results demonstrate that Hspd1 is an essential gene for early embryonic development in mice, while reducing the amount of Hsp60 by inactivation of one allele of the gene is compatible with survival to term as well as postnatal life. ..
  41. TEHVER R, Chen J, Thirumalai D. Allostery wiring diagrams in the transitions that drive the GroEL reaction cycle. J Mol Biol. 2009;387:390-406 pubmed publisher
    ..We find that several substrate protein binding residues as well as sites related to ATPase activity belong to a single functional network in GroEL. For GroES, the mobile loop residues and GroES/GroES interface residues are linked. ..
  42. Tyagi N, Fenton W, Deniz A, Horwich A. Double mutant MBP refolds at same rate in free solution as inside the GroEL/GroES chaperonin chamber when aggregation in free solution is prevented. FEBS Lett. 2011;585:1969-72 pubmed publisher
    ..The GroEL/GroES chamber thus appears to function passively toward DM-MBP. ..
  43. 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
    ..Altering the net-negative charge of the GroEL cage wall also strongly affected chaperonin function. Based on these findings, the GroEL/GroES compartment is essential for protein folding in vivo. ..
  44. Taguchi H. Chaperonin GroEL meets the substrate protein as a "load" of the rings. J Biochem. 2005;137:543-9 pubmed
    ..Finally I propose the mechanistic similarity between GroEL and kinesin, a molecular motor that moves along a microtubule in an ATP-dependent manner. ..
  45. Taguchi H, Tsukuda K, Motojima F, Koike Takeshita A, Yoshida M. BeF(x) stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers. J Biol Chem. 2004;279:45737-43 pubmed
    ..Thus, BeF(x) stabilizes two GroEL-GroES complexes; one with a single folding chamber and the other with double folding chambers. These results shed light on the intermediate ADP.P(i) nucleotide states in the functional cycle of GroEL. ..
  46. Fenton W, Horwich A. Chaperonin-mediated protein folding: fate of substrate polypeptide. Q Rev Biophys. 2003;36:229-56 pubmed
  47. Marchenko N, Marchenkov V, Kotova N, Semisotnov G, Bulankina N, Kaliman P. [Effect of ADP and GroES on interaction of molecular chaperonin GroEL with non-native lysozyme]. Ukr Biokhim Zh (1999). 2003;75:88-94 pubmed
    ..e. the formation of the complex of GroEL with GroES) leads to drastic weakness of the interaction of GroEL with nonnative lysozyme and the efficiency of its aggregation becomes comparable with that in the absence of GroEL. ..
  48. Fossati G, Izzo G, Rizzi E, Gancia E, Modena D, Moras M, et al. Mycobacterium tuberculosis chaperonin 10 is secreted in the macrophage phagosome: is secretion due to dissociation and adoption of a partially helical structure at the membrane?. J Bacteriol. 2003;185:4256-67 pubmed
    To confirm that Mycobacterium tuberculosis chaperonin 10 (Cpn10) is secreted outside the live bacillus, infected macrophages were examined by electron microscopy...
  49. Levy Rimler G, Bell R, Ben Tal N, Azem A. Type I chaperonins: not all are created equal. FEBS Lett. 2002;529:1-5 pubmed
    ..This review focuses on the unique properties of organellar chaperonins. ..
  50. Broadley S, Vanags D, Williams B, Johnson B, Feeney D, Griffiths L, et al. Results of a phase IIa clinical trial of an anti-inflammatory molecule, chaperonin 10, in multiple sclerosis. Mult Scler. 2009;15:329-36 pubmed publisher
    b>Chaperonin 10 (Cpn10) is a mitochondrial molecule involved in protein folding. The aim of this study was to determine the safety profile of Cpn10 in patients with multiple sclerosis (MS).
  51. Dutta R, Jha R, Gupta S, Gupta R, Salhan S, Mittal A. Seroprevalence of antibodies to conserved regions of Chlamydia trachomatis heat shock proteins 60 and 10 in women in India. Br J Biomed Sci. 2007;64:78-83 pubmed
    ..001) and at 1 in 6250 (P < 0.01). ..
  52. Dadamessi I, Eb F, Betsou F. Combined detection of Chlamydia trachomatis-specific antibodies against the 10 and 60-kDa heat shock proteins as a diagnostic tool for tubal factor infertility: Results from a case-control study in Cameroon. FEMS Immunol Med Microbiol. 2005;45:31-5 pubmed
    ..01). The detection of either C. trachomatis-associated anti-Chsp10 or anti-Chsp60 antibodies cumulatively allowed specific diagnosis of secondary infertility (57.4% sensitivity, 75.5% specificity). ..
  53. Yang E, Guo J, Diehl G, DeSouza L, Rodrigues M, Romaschin A, et al. Protein expression profiling of endometrial malignancies reveals a new tumor marker: chaperonin 10. J Proteome Res. 2004;3:636-43 pubmed
    ..cation exchange chromatography and displaying enhanced expression in these malignant tissues was identified as chaperonin 10. The increased expression of chaperonin 10 in malignant endometrial tissues was further confirmed by parallel ..