Archaeal chaperonins

Frontiers in Bioscience

Volumn 14, Issue 4, 2009, Pages 1304-1324

  Large, Andrew T ^a   Lund, Peter A ^a  

^a UNIVERSITY OF BIRMINGHAM   (United Kingdom)

Author keywords

Archaea; Cct; Chaperonin; Groel; Molecular chaperone; Protein folding; Review; Thermosome

Indexed keywords

ARCHAEA; BACTERIA (MICROORGANISMS); EUKARYOTA;

CHAPERONIN;

ARCHAEBACTERIUM; CHEMICAL STRUCTURE; CHEMISTRY; CLASSIFICATION; PHYLOGENY; PHYSIOLOGY; PROTEIN CONFORMATION; REVIEW;

ARCHAEA; CHAPERONINS; MODELS, MOLECULAR; PHYLOGENY; PROTEIN CONFORMATION;

EID: 63849276112     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/3310     Document Type: Article

References (168)

1. Anfinsen, C. B.: Principles that govern the folding of protein chains. Science 181, 223-230 (1973).
2. Pelham, H. R.: Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell 46, 959-961 (1986). (Pubitemid 17182721)
3. Ellis, R. J.: Proteins as molecular chaperones. Nature 328, 378-379 (1987).
4. Rothman, J. E.: Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cell 59, 591-601 (1989). (Pubitemid 19282866)
5. Ellis, R. J.: Molecular chaperones: assisting assembly in addition to folding. Trends Biochem Sci 31, 395-401 (2006). (Pubitemid 44038913)
6. Hartl, F. U., & M. Hayer-Hartl: Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295 1852-1858 (2002). (Pubitemid 34214115)
7. Macario, A. J. L., & E. Conway de Macario: Molecular chaperones: multiple functions, pathologies, and potential applications. Front Biosci 12, 2588-2600 (2007).
8. R. Qamra, V. Srinivas & S. C. Mande: Mycobacterium tuberculosis GroEL homologues unusually exist as lower oligomers and retain the ability to suppress aggregation of substrate proteins. J Mol Biol 342, 605-617 (2004). (Pubitemid 39149762)
9. Ellis, R. J.: Molecular Chaperones: The Plant Connection. Science 250, 954-959 (1990). (Pubitemid 120031795)
10. Reading, D. S., R. L. Hallberg & A. M. Myers: Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor. Nature 337, 655-659 (1989).
11. Bui, E. T., P. J. Bradley & P. J. Johnson: A common evolutionary origin for mitochondria and hydrogenosomes. Proc Natl Acad Sci USA 93, 9651-9656 (1996). (Pubitemid 26296663)
12. Hemmingsen, S. M., C. Woolford, S. M. van der Vies, K. Tilly, D. T. Dennis, C. P. Georgopoulos, R. W. Hendrix, & R. J, Ellis: Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature 333, 330- 334 (1988).
13. Nielsen, K. L., N. McLennan, M. Masters & N. J. Cowan: A single-ring mitochondrial chaperonin (Hsp60- Hsp10) can substitute for GroEL-GroES in vivo. J Bacteriol 181, 5871-5875 (1999). (Pubitemid 29437165)
14. Braig, K., Z. Otwinowski, R. Hegde, D.C. Boisvert, A. Joachimiak, A. L. Horwich & P.B. Sigler: The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature 371, 578-586 (1994).
15. Ditzel, L., J. Löwe, D. Stock, K.O. Stetter, H. Huber, R. Huber & S. Steinbacher: Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93, 125-138 (1998). (Pubitemid 28173558)
16. Shomura, Y., T. Yoshida, R. Iizuka, T. Maruyama, M. Yohda & K. Miki: Crystal structures of the group II chaperonin from Thermococcus strain KS-1: steric hindrance by the substituted amino acid, and inter-subunit rearrangement between two crystal forms. J Mol Biol 335, 1265-1278 (2004). (Pubitemid 38081291)
17. Llorca, O., M. G. Smyth, J. L. Carrascosa, K. R. Willison, M. Radermacher, S. Steinbacher & J. M. Valpuesta: 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin. Nature Struct Biol 6, 639-642 (1999). (Pubitemid 29318952)
18. Coates, A. R., T. M. Shinnick, & R. J. Ellis: Chaperonin nomenclature Mol Microbiol 8, 787 (1993).
19. Silver, L. M., M. White & K. Artzt: Evidence for unequal crossing over within the mouse T/t complex. Proc Natl Acad Sci USA 77, 6077-6080 (1980). (Pubitemid 11206344)
20. Phipps, B. M., D. Typke, R. Heger, S. Volker, A. Hoffmann, K. O. Stetter & W. Baumeister: Structure of a molecular chaperone from a thermophilic archaebacterium Nature 361, 475-477 (1993). (Pubitemid 23050141)
21. Trent, J. D., E. Nimmesgern, J. S. Wall, F. U. Hartl & A. L. Horwich: A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein tcomplex polypeptide-1. Nature 354, 490-493 (1991). (Pubitemid 21896866)
22. Kagawa, H. K., J. Osipiuk, N. Maltsev, R. Overbeek, E. Quaite-Randall, A. Joachimiak & J. D. Trent: The 60 kDa heat shock proteins in the hyperthermophilic archaeon Sulfolobus shibatae. J Mol Biol 253, 712-725 (1995).
23. Quaite-Randall, E., J. D. Trent, R. Josephs & A. Joachimiak, : Conformational cycle of the archaeosome, a TCP1-like chaperonin from Sulfolobus shibatae. J Biol Chem 270, 28818-28823 (1995).
24. Kuo, Y. P., D. K. Thompson, A. St Jean, R. L. Charlebois & C. J. Daniels: Characterization of two heat shock genes from Haloferax volcanii: a model system for transcription regulation in the Archaea. J Bacteriol 179, 6318-6324 (1997). (Pubitemid 27443912)
25. Georgopoulos, C. P., R. W. Hendrix, A. D Kaiser, & W. B. Wood: Role of the host cell in bacteriophage morphogenesis: effects of a bacterial mutation on T4 head assembly. Nature New Biol 239, 38-41 (1972).
26. Takano, T., & T. Kakefuda: Involvement of a bacterial factor in morphogenesis of bacteriophage capsid. Nature New Biol 239, 34-37 (1972).
27. Fayet, O., T. Ziegelhoffer & C. Georgopoulos: The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J Bacteriol 171, 1379-1385 (1989). (Pubitemid 19080775)
28. Kusukawa, N., & T. Yura: Heat shock protein GroE of Escherichia coli: key protective roles against thermal stress. Genes Dev 2, 874-882 (1988).
29. Gragerov, A., E. Nudler, N. Komissarova, G. A. Gaitanaris, M. E. Gottesman & V. Nikiforov : Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli. Proc Natl Acad Sci USA 89, 10341- 10344 (1992).
30. Goloubinoff, P., A. A. Gatenby, & G. H. Lorimer: GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature 337, 44-47 (1989). (Pubitemid 19022550)
31. Van Dyk, T. K., A. A. Gatenby & R. A. LaRossa: Demonstration by genetic suppression of interaction of GroE products with many proteins. Nature 342, 451-453 (1989). (Pubitemid 19277524)
32. Ewalt, K. L., J. P. Hendrick, W. A. Houry & F. U Hartl: In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell 90, 491-500 (1997). (Pubitemid 27347239)
33. Houry, W. A., D. Frishman, C. Eckerskorn, F. Lottspeich & F. U. Hartl: Identification of in vivo substrates of the chaperonin GroEL. Nature 402, 147-154 (1999).
34. Kerner, M. J., D. J. Naylor, Y. Ishihama, T. Maier, H. C. Chang, A. P. Stines, C. Georgopoulos, D. Frishman, M. Hayer-Hartl, M. Mann & F. U. Hartl: Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell 122, 209-220 (2005). (Pubitemid 41032985)
35. Chapman, E., G. W. Farr, R. Usaite, K. Furtak, W. A. Fenton, T. K. Chaudhuri, E. R. Hondorp, R. G. Matthews, S. G. Wolf, J. R. Yates, M. Pypaert & A. L. Horwich: Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL. Proc Natl Acad Sci USA 103, 15800-15805 (2006). (Pubitemid 44657547)
36. Horwich, A. L., W. A. Fenton, E. Chapman & G. W. Farr: Two families of chaperonin: physiology and mechanism. Annu Rev Cell Dev Biol 23, 115-145 (2007).
37. Shimamura, T., A. Koike-Takeshita, K. Yokoyama, R. Masui, N. Murai, M. Yoshida, H. Taguchi & S. Iwata: Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity. Structure 12, 1471-1480 (2004). (Pubitemid 39092091)
38. Endo, A., & Y. Kurusu: Identification of in vivo substrates of the chaperonin GroEL from Bacillus subtilis. Biosci Biotechnol Biochem 71, 1073-1077 (2007). (Pubitemid 46650932)
39. Noivirt-Brik, O., R. Unger & A. Horovitz: Low folding propensity and high translation efficiency distinguish in vivo substrates of GroEL from other Escherichia coli proteins. Bioinformatics 23, 3276-3279 (2007). (Pubitemid 350238878)
40. Lin, Z., & H. S. Rye: GroEL-mediated protein folding: making the impossible, possible. Crit Rev Biochem Mol Biol 41, 211-239 (2006). (Pubitemid 44100582)
41. Thirumalai, D., & G. H. Lorimer: Chaperoninmediated protein folding. Annu Rev Biophys Biomol Struct 30, 245-269 (2001).
42. Stan, G., D. Thirumalai, G. H. Lorimer & B. R. Brooks: Annealing function of GroEL: structural and bioinformatic analysis. Biophys Chem. 100, 453-467 (2003). (Pubitemid 36338058)
43. Sharma, S., K. Chakraborty, B. K. Müller, N. Astola, Y. C. Tang, D. C. Lamb, M. Hayer-Hartl & F. U. Hartl: Monitoring protein conformation along the pathway of chaperonin-assisted folding. Cell. 133, 142-153 (2008). (Pubitemid 351442991)
44. Lin, Z., D. Madan & H. S. Rye: GroEL stimulates protein folding through forced unfolding. Nat Struct Mol Biol 15, 303-311 (2008). (Pubitemid 351654048)
45. Ellis, R. J.: Protein folding: importance of the Anfinsen cage. Current Biol 13, 881-883 (2003).
46. Tang, Y.C., H. C. Chang, A. Roeben, D. Wischnewski, N. Wischnewski, M. J. Kerner, F. U. Hartl & M. Hayer-Hartl: Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Cell 125, 903-914 (2006). (Pubitemid 43795198)
47. Yifrach, O., & A. Horovitz: Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. Biochemistry 34, 5303-5308 (1995).
48. Horovitz, A., Y. Fridmann, G. Kafri & O. Yifrach: Review: allostery in chaperonins. J Struct Biol 135, 104-114 (2001).
49. Rye, H.S., S. G. Burston, W. A. Fenton, J. M. Beechem, Z. Xu, P. B. Sigler & A. L. Horwich: Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature 388, 792-798 (1997). (Pubitemid 27375160)
50. Rye, H. S., A. M. Roseman, S. Chen, K. Furtak, W. A. Fenton, H. R. Saibil & A. L. Horwich: GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of foldingactive rings. Cell 97, 325-338 (1999). (Pubitemid 29214589)
51. Nielsen, K. L., & N. J. Cowan : A single ring is sufficient for productive chaperonin-mediated folding in vivo. Mol Cell 2, 93-99 (1998). (Pubitemid 128378970)
52. Qamra, R., S. C. Mande, A. R. Coates & B. Henderson: The unusual chaperonins of Mycobacterium tuberculosis. Tuberculosis (Edinb) 85, 385-394 (2005). (Pubitemid 41617393)
53. Henderson, B., E. Allan, & A. R. Coates: Stress wars: the direct role of host and bacterial molecular chaperones in bacterial infection. Infect Immun 74, 3693-3706 (2006). (Pubitemid 43993301)
54. Liou A. K., & K. R. Willison: Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes. EMBO J 16, 4311-4316 (1997). (Pubitemid 27298184)
55. Martín-Benito, J., J. Grantham, J. Boskovic, K. I. Brackley, J. L. Carrascosa, K. R. Willison & J. M. Valpuesta: The inter-ring arrangement of the cytosolic chaperonin CCT. EMBO reports 8, 252-257 (2007). (Pubitemid 46344590)
56. Archibald, J. M., J. M. Logsdon Jr, & W. F. Doolittle: Origin and evolution of eukaryotic chaperonins: phylogenetic evidence for ancient duplications in CCT genes. Mol Biol Evol 17, 1456-1466 (2000).
57. Fares, M. A., & K. H. Wolfe: Positive selection and subfunctionalization of duplicated CCT chaperonin subunits. Mol Biol Evol 20, 1588-1597 (2003). (Pubitemid 41070819)
58. Stoldt, V., F. Rademacher, V. Kehren, J. F. Ernst, D. A. Pearce & F. Sherman: Review: the Cct eukaryotic chaperonin subunits of Saccharomyces cerevisiae and other yeasts. Yeast 12, 523-529 (1996).
59. Lundin, V. F., M. Srayko, A. A. Hyman & M. R. Leroux: Efficient chaperone-mediated tubulin biogenesis is essential for cell division and cell migration in C. elegans. Dev Biol 313, 320-334 (2008). (Pubitemid 50007754)
60. Gao, Y., J. O. Thomas, R. L. Chow, G. H. Lee & N. J. Cowan: A cytoplasmic chaperonin that catalyzes beta-actin folding. Cell 69, 1043-1050 (1992).
61. Yaffe, M. B,, G. W. Farr, D. Miklos, A. L. Horwich, M. L. Sternlicht & H. Sternlicht: TCP1 complex is a molecular chaperone in tubulin biogenesis. Nature 358, 245-248 (1992).
62. Sternlicht H., G. W. Farr, M. L. Sternlicht, J. K. Driscoll, K. Willison & M. B. Yaffe: The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo. Proc Natl Acad Sci U S A 90, 9422-9426 (1993). (Pubitemid 23315796)
63. Vinh, D. B., & D. G. Drubin: A yeast TCP-1-like protein is required for actin function in vivo. Proc Natl Acad Sci U S A 91, 9116-9120 (1994).
64. Ursic, D., J. C. Sedbrook, K. L. Himmel & M. R. Culbertson: The essential yeast Tcp1 protein affects actin and microtubules. Mol Biol Cell 5, 1065-1080 (1994) (Pubitemid 24356622)
65. Llorca, O., E. A. McCormack, G. Hynes, J. Grantham, J. Cordell, J. L. Carrascosa, K. R. Willison, J. J. Fernandez & J. M. Valpuesta: Eukaryotic type II chaperonin CCT interacts with actin through specific subunits. Nature 402, 693-696 (1999). (Pubitemid 129516343)
66. Llorca, O., J. Martín-Benito, M. Ritco-Vonsovici, J. Grantham, G. M. Hynes, K. R. Willison, J. L. Carrascosa & J. M. Valpuesta : Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi-native conformations. EMBO J 5971-5979 (2000).
67. Spiess, C., A. S. Meyer, S. Reissmann & J. Frydman: Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. Trends Cell Biol 14, 598-604 (2004). (Pubitemid 39440608)
68. Craig, E. A.: Eukaryotic chaperonins: lubricating the folding of WD-repeat proteins Curr Biol 13, 904-905 (2003).
69. Geissler, S., K. Siegers & E. Schiebel: A novel protein complex promoting formation of functional alpha- and gamma-tubulin. EMBO J 17, 952-966 (1998). (Pubitemid 28077650)
70. Vainberg, I. E., S. A. Lewis, H. Rommelaere, C. Ampe, J. Vandekerckhove, H. L. Klein & N. J. Cowan: Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin. Cell 93, 863-873 (1998). (Pubitemid 28257591)
71. Lewis, V.A., G. M. Hynes, D. Zheng, H. Saibil & K. Willison: T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol. Nature 358, 249-252 (1992).
72. Llorca, O., M. G. Smyth, S. Marco, J. L. Carrascosa, K. R. Willison & J. M. Valpuesta: ATP binding induces large conformational changes in the apical and equatorial domains of the eukaryotic chaperonin containing TCP-1 complex. J Biol Chem 273, 10091-10094 (1998). (Pubitemid 28227605)
73. Kafri, G., K. R. Willison & A. Horovitz: Nested allosteric interactions in the cytoplasmic chaperonin containing TCP-1. Protein Sci 10, 445-449 (2001). (Pubitemid 32225664)
74. Rivenzon-Segal, D., S. G. Wolf, L. Shimon, K. R. Willison & A. Horovitz: Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis. Nat Struct Mol Biol 12, 233-237 (2005). (Pubitemid 43079364)
75. Meyer, A., J. Gillespie, D. Walther, I. Millet, S. Doniach & J. Frydman: Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis. Cell 113, 369-381 (2003). (Pubitemid 36556118)
76. May, R. C., & L. M. Machesky: Phagocytosis and the actin cytoskeleton. J Cell Sci 114, 1061-1077 (2001). (Pubitemid 32288521)
77. Mitchison, T. J.: Evolution of a dynamic cytoskeleton. Philos Trans R Soc Lond B Biol Sci 349, 299-304 (1995).
78. Soppa, J.: From genomes to function: haloarchaea as model organisms. Microbiology 152, 585-590 (2006).
79. Kapatai, G., A. Large, J. L. Benesch, C. V. Robinson, J. L. Carrascosa, J. M. Valpuesta, P. Gowrinathan & P. A. Lund: All three chaperonin genes in the archaeon Haloferax volcanii are individually dispensable. Molec Microbiol 61, 1583-1597 (2006). (Pubitemid 44359385)
80. Emmerhoff, O.J., H. P. Klenk & N. K. Birkeland: Characterization and sequence comparison of temperatureregulated chaperonins from the hyperthermophilic archaeon Archaeoglobus fulgidus. Gene 215, 431-438 (1998). (Pubitemid 28382946)
81. Kagawa, H. K., T. Yaoi, K. Brocchieri, R. A. McMillan, T. Alton & J. D. Trent: The composition, structure and stability of a group II chaperonin are temperature regulated in a hyperthermophilic archaeon. Molec Microbiol 48, 143-156 (2003). (Pubitemid 36411473)
82. Shockley, K. R., D. E. Ward, S. R. Chhabra, S. B. Conners, C. I. Montero & R. M. Kelly: Heat shock response by the hyperthermophilic archaeon Pyrococcus furiosus. Appl Environ Microbiol 69, 2365-2371 (2003). (Pubitemid 36443659)
83. Boonyaratanakornkit, B. B., A. J. Simpson, T. A. Whitehead, C. M. Fraser, N. M. El-Sayed & D. S. Clark: Transcriptional profiling of the hyperthermophilic methanarchaeon Methanococcus jannaschii in response to lethal heat and non-lethal cold shock. Environ Microbiol 7, 789-797 (2005). (Pubitemid 40697637)
84. Shukla, H. D.: Proteomic analysis of acidic chaperones, and stress proteins in extreme halophile Halobacterium NRC-1: a comparative proteomic approach to study heat shock response. Proteome Sci 4, 6 (2006).
85. Rohlin, L., J. D. Trent, K. Salmon, U. Kim, R. P. Gunsalus & J. C. Liao: Heat shock response of Archaeoglobus fulgidus. J Bacteriol 187, 6046-6057 (2005). (Pubitemid 41262802)
86. Zhang, W., D. E. Culley, L. Nie & F. J. Brockman: DNA microarray analysis of anaerobic Methanosarcina barkeri reveals responses to heat shock and air exposure. J Ind Microbiol Biotech 33, 784-790 (2006). (Pubitemid 44106685)
87. Coker, J. A., P. Dassarma, J. Kumar, J. A. Müller & S. Dassarma: Transcriptional profiling of the model archaeon Halobacterium sp. NRC-1: responses to changes in salinity and temperature. Saline Systems 3, 6 (2007).
88. Marteinsson, V. T., A. L. Reysenbach, J. L. Birrien & D. Prieur: A stress protein is induced in the deep-sea barophilic hyperthermophile Thermococcus barophilus when grown under atmospheric pressure. Extremophiles 3, 277-282 (1999). (Pubitemid 30000830)
89. Baker-Austin, C., M. Dopson, M. Wexler, R. G. Sawers, A. Stemmler, B. P. Rosen & P. L. Bond: Extreme arsenic resistance by the acidophilic archaeon 'Ferroplasma acidarmanus' Fer1. Extremophiles 11, 425-434 (2007). (Pubitemid 46742125)
90. Karlin, S., J. Mrázek, J. Ma & L Brocchieri: Predicted highly expressed genes in archaeal genomes. Proc Natl Acad Sci U S A 102, 7303-7308 (2005). (Pubitemid 40696374)
91. Trent, J. D., H. K. Kagawa, T. Yaoi, E. Olle, & N. J. Zaluzec: Chaperonin filaments: the archaeal cytoskeleton? Proc Natl Acad Sci USA 94, 5383-5388 (1997). (Pubitemid 27214792)
92. Trent, J. D., H. K. Kagawa, C. D. Paavola, R. A. McMillan, J. Howard, L. Jahnke, C. Lavin, T. Embaye & C. E. Henze: Intracellular localization of a group II chaperonin indicates a membrane-related function. Proc Natl Acad Sci USA 100, 15589-15594 (2003). (Pubitemid 38021034)
93. Ruggero, D., A. Ciammaruconi & P. Londei: The chaperonin of the archaeon Sulfolobus solfataricus is an RNA-binding protein that participates in ribosomal RNA processing. EMBO J 17, 3471-3477 (1998). (Pubitemid 28279519)
94. Evguenieva-Hackenberg, E., P. Walter, E. Hochleitner, F. Lottspeich & G. Klug: An exosome-like complex in Sulfolobus solfataricus. EMBO RepD53 4, 889-893 (2003). (Pubitemid 37309279)
95. Balczun, C., A. Bunse, C. Schwarz, M. Piotrowski & U. Kück: Chloroplast heat shock protein Cpn60 from Chlamydomonas reinhardtii exhibits a novel function as a group II intron-specific RNA-binding protein. FEBS Letters 580, 4527-4532 (2006). (Pubitemid 44118277)
96. Sanyal, A., A. Harington, C. J. Herbert, O. Groudinsky, P. P. Slonimski, B. Tung & G. S. Getz: Heat shock protein HSP60 can alleviate the phenotype of mitochondrial RNAdeficient temperature-sensitive mna2 pet mutants. Mol Gen Genet 246, 56-54 (1995).
97. Archibald, J. M., J. M. Logsdon & W. F. Doolittle: Recurrent paralogy in the evolution of archaeal chaperonins. Curr Biol 9, 1053-1056 (1999). (Pubitemid 29456177)
98. Archibald, J. M., & A. J. Roger: Gene duplication and gene conversion shape the evolution of archaeal chaperonins. J Mol Biol 316, 1041-1050 (2002). (Pubitemid 34729223)
99. Ruano-Rubio, V., & M. A. Fares: Testing the neutral fixation of hetero-oligomerism in the archaeal chaperonin CCT. Mol Biol Evol 24, 1384-1396 (2007). (Pubitemid 47343947)
100. Large, A., C. Stamme, C. Lange, Z. Duan, T. Allers, J. Soppa & P. A. Lund: Characterization of a tightly controlled promoter of the halophilic archaeon Haloferax volcanii and its use in the analysis of the essential cct1 gene. Mol Microbiol 66, 1092-1106 (2007). (Pubitemid 350115018)
101. Izumi, M., S. Fujiwara, M. Takagi, K. Fukui & T. Imanaka: Two kinds of archaeal chaperonin with different temperature dependency from a hyperthermophile. Biochem Biophys Res Commun 280, 581-587 (2001). (Pubitemid 32912831)
102. Yoshida, T., A. Ideno, S. Hiyamuta, M. Yohda & T. Maruyama: Natural chaperonin of the hyperthermophilic archaeum, Thermococcus strain KS-1: a hetero-oligomeric chaperonin with variable subunit composition. Mol Microbiol 39, 1406-1413 (2001). (Pubitemid 32225148)
103. Yoshida, T., A. Ideno, R. Suzuki, M. Yohda & T. Maruyama: Two kinds of archaeal group II chaperonin subunits with different thermostability in Thermococcus strain KS-1. Mol Microbiol 44, 761-769 (2002). (Pubitemid 34526586)
104. Yoshida, T., T. Kanzaki, R. Iizuka, T. Komada, T. Zako, R. Suzuki, T. Maruyama & M. Yohda: Contribution of the C-terminal region to the thermostability of the archaeal group II chaperonin from Thermococcus sp. strain KS-1. Extremophiles 10, 451-459 (2006). (Pubitemid 44564008)
105. Galagan, J.E., C. Nusbaum, A. Roy, M. G. Endrizzi, P. Macdonald, W. FitzHugh, S. Calvo, R. Engels, S. Smirnov, D. Atnoor, A. Brown, N. Allen, J. Naylor, N. Stange-Thomann, K. DeArellano, R. Johnson, L. Linton, P. McEwan, K. McKernan, J. Talamas, A. Tirrel, W. Ye, A. Zimmer, R. D. Barber, I. Cann, D. E. Graham, D. A. Grahame, A. M. Guss, R. Hedderich, C. Ingram-Smith, H. C. Kuettner, J. A. Krzycki, J. A. Leigh, W. Li, J. Liu, B. Mukhopadhyay, J. N. Reeve, K. Smith, T. A. Springer, L. A. Umayam, O. White, R. H. White, E. Conway de Macario, J. G. Ferry, K. F. Jarrell, H. Jing, A. J. L. Macario, I. Paulsen, M. Pritchett, K. R. Sowers, R. V. Swanson, S. H. Zinder, E. Lander, W. W. Metcalf, & B. Birren : The genome of M. acetivorans reveals extensive metabolic and physiological diversity. Genome Res 12, 532-542 (2002). (Pubitemid 34308633)
106. Conway de Macario, E., D. L. Maeder & A. J. L. Macario: Breaking the mould: archaea with all four chaperoning systems. Biochem Biophys Res Commun 301, 811-812 (2003). (Pubitemid 36279185)
107. Klunker, D., B. Haas, A. Hirtreiter, L. Figueiredo, D. J. Naylor, G. Pfeifer, V. Müller, U. Deppenmeier, G. Gottschalk, F. U. Hartl, & M. Hayer-Hartl: Coexistence of group I and group II chaperonins in the archaeon Methanosarcina mazei. J Biol Chem 278, 33256-33267 (2003). (Pubitemid 37055775)
108. Shih, C. J., & M. C. Lai: Analysis of the AAA+ chaperone clpB gene and stress-response expression in the halophilic methanogenic archaeon Methanohalophilus portucalensis. Microbiology 153, 2572-2583 (2007).
109. Maeder, D. L., A. J. Macario, & E. C. de Macario: Novel chaperonins in a prokaryote. J Mol Evol 60, 409-416 (2005). (Pubitemid 40691213)
110. Nesbø, C. L., S. L'Haridon, K. O. Stetter & W. F. Doolittle: Phylogenetic analyses of two "archaeal" genes in Thermotoga maritima reveal multiple transfers between archaea and bacteria. Mol Biol Evol 18, 362-375 (2001). (Pubitemid 32225085)
111. Figueiredo L., D. Klunker, D. Ang, D. J. Naylor, M. J. Kerner, C. Georgopoulos, F. U. Hartl, & M. Hayer-Hartl: Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation. J Biol Chem 279, 1090-1099 (2004). (Pubitemid 38082630)
112. Nitsch, M., M. Klumpp, A. Lupas & W. Baumeister: The thermosome: alternating alpha and beta-subunits within the chaperonin of the archaeon. Thermoplasma acidophilum J Mol Biol 267, 142-149 (1997). (Pubitemid 27149743)
113. Iizuka, R., T. Yoshida, N. Ishii, T. Zako, K. Takahashi, K. Maki, T. Inobe, K. Kuwajima & M. Yohda: Characterization of archaeal group II chaperonin-ADPmetal fluoride complexes: implications that group II chaperonins operate as a "two-stroke engine". J Biol Chem 280, 40375-40383 (2005). (Pubitemid 41779175)
114. Nitsch, M., J. Walz, D. Typke, M. Klumpp, L. O. Essen & W. Baumeister: Group II chaperonin in an open conformation examined by electron tomography. Nature Struct Biol 5, 855-857 (1998). (Pubitemid 28467404)
115. Schoehn, G., E. Quaite-Randall, J. L. Jiménez, A. Joachimiak A & H. R. Saibil: Three conformations of an archaeal chaperonin, TF55 from Sulfolobus shibatae. J Mol Biol 296, 813-819 (2000).
116. Schoehn, G., M. Hayes, M. Cliff, A. R. Clarke, & H. R. Saibil: Domain rotations between open, closed and bulletshaped forms of the thermosome, an archaeal chaperonin. J Mol Biol 301, 323-332 (2000).
117. Iizuka, R., S. So, T. Inobe, T. Yoshida, T. Zako, K. Kuwajima & M. Yohda: Role of the helical protrusion in the conformational change and molecular chaperone activity of the archaeal group II chaperonin J Biol Chem 279, 18834-18839 (2004). (Pubitemid 38623310)
118. Iizuka, R., T. Yoshida, N. Ishii, T. Zako, K. Takahashi, K. Maki, T. Inobe, K. Kuwajima & M. Yohda: Characterization of archaeal group II chaperonin-ADP-metal fluoride complexes: implications that group II chaperonins operate as a "two-stroke engine". J Biol Chem 280, 40375- 40383 (2005). (Pubitemid 41779175)
119. Gutsche, I., J. Holzinger, M. Rössle, H. Heumann, W. Baumeister & R. P. May: Conformational rearrangements of an archaeal chaperonin upon ATPase cycling. Curr Biol 10, 405-408 (2000). (Pubitemid 30213388)
120. Gutsche I., J. Holzinger, N. Rauh, W. Baumeister & R. P. May: ATP-induced structural change of the thermosome is temperature-dependent J Struct Biol 135, 139-146 (2001).
121. Andrä, S., G. Frey, R. Jaenicke & K. O. Stetter: The thermosome from Methanopyrus kandleri possesses an NH4+- dependent ATPase activity. Eur J Biochem 255, 93-99 (1998). (Pubitemid 28316840)
122. Son, H. J., E. J. Shin, S. W. Nam, D. E. Kim & S. J. Jeon: Properties of the alpha subunit of a chaperonin from the hyperthermophilic crenarchaeon Aeropyrum pernix K1 FEMS Microbiol Lett 266, 103-109 (2007).
123. Large, A.T., E. Kovacs & P. A. Lund: Properties of the chaperonin complex from the halophilic archaeon Haloferax volcanii. FEBS Lett 532, 309-312 (2002). (Pubitemid 35441366)
124. Hongo, K., H. Hirai, C. Uemura, S. Ono, J. Tsunemi, T. Higurashi, T. Mizobata & Y. Kawata: A novel ATP/ADP hydrolysis activity of hyperthermostable group II chaperonin in the presence of cobalt or manganese ion. FEBS Lett 580, 34-40 (2006). (Pubitemid 43005308)
125. Chen, H. Y., Z. M. Chu, Y. H. Ma, Y. Zhang & S. L. Yang: Expression and characterization of the chaperonin molecular machine from the hyperthermophilic archaeon Pyrococcus furiosus. J Basic Microbiol 47, 132-137 (2007). (Pubitemid 46953812)
126. Furutani, M., T. Iida, T. Yoshida & T. Maruyama: Group II chaperonin in a thermophilic methanogen, Methanococcus thermolithotrophicus: Chaperone activity and filament-forming ability. J Biol Chem 273, 28399- 28407 (1998). (Pubitemid 28496144)
127. Yoshida, T., R. Kawaguchi & T. Maruyama: Nucleotide specificity of an archaeal group II chaperonin from Thermococcus strain KS-1 with reference to the ATPdependent protein folding cycle. FEBS Lett 514, 269-274 (2002). (Pubitemid 34273952)
128. Kusmierczyk, A. R., & J. Martin: Nested cooperativity and salt dependence of the ATPase activity of the archaeal chaperonin Mm-cpn. FEBS Lett 547, 201-204 (2003). (Pubitemid 36829406)
129. Horovitz, A., & K. R. Willison: Allosteric regulation of chaperonins. Curr Op Struct Biol 15, 646-651 (2005). (Pubitemid 41668520)
130. Shimon, L., G. M. Hynes, E. A. McCormack, K. R. Willison & A. Horovitz: ATP-Induced allostery in the eukaryotic chaperonin CCT is abolished by the mutation G345D in CCT4 that renders yeast temperature-sensitive for growth. J Mol Biol 377, 469-477 (2008).
131. Bigotti, M. G., & A. R. Clarke: Cooperativity in the thermosome. J Mol Biol 348, 13-26 (2005). (Pubitemid 40461837)
132. Kusmierczyk, A. R., & J. Martin: Nucleotidedependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis. Biochem J 371, 669-673 (2003). (Pubitemid 36578866)
133. Okochi, M., H. Matsuzaki, T. Nomura, N. Ishii & M. Yohda: Molecular characterization of the group II chaperonin from the hyperthermophilic archaeum Pyrococcus horikoshii OT3. Extremophiles 9, 127-134 (2005). (Pubitemid 40660352)
134. Iizuka, R., T. Yoshida, T. Maruyama, Y. Shomura, K. Miki & M. Yohda: Glycine at the 65th position plays an essential role in ATP-dependent protein folding by archael group II chaperonin. Biochem Biophys Res Commun 289, 1118-1124 (2001). (Pubitemid 34076307)
135. Guagliardi, A., L. Cerchia, S. Bartolucci & M. Rossi: The chaperonin from the archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro. Protein Sci 3, 1436-1443 (1994). (Pubitemid 24314463)
136. Yoshida, T., R. Iizuka, K. Itami, T. Yasunaga, H. Sakuraba, T. Ohshima, M. Yohda & T. Maruyama: Comparative analysis of the protein folding activities of two chaperonin subunits of Thermococcus strain KS-1: the effects of beryllium fluoride. Extremophiles 11, 225-235 (2007).
137. Pappenberger, G., J. A. Wilsher, S. M. Roe, D. J. Counsell, K. R. Willison & L.H. Pearl: Crystal structure of the CCTgamma apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin. J Mol Biol 318, 1367-1379 (2002). (Pubitemid 34754004)
138. McCormack, E. A., M. J. Rohman & K. R. Willison: Mutational screen identifies critical amino acid residues of beta-actin mediating interaction between its folding intermediates and eukaryotic cytosolic chaperonin CCT. J Struct Biol 135, 185-197 (2001).
139. Hynes, G. M., & K. R. Willison: Individual subunits of the eukaryotic cytosolic chaperonin mediate interactions with binding sites located on subdomains of beta-actin. J Biol Chem 275, 18985-18994 (2000). (Pubitemid 30422864)
140. Rommelaere, H., M. De Neve, R. Melki, J. Vandekerckhove & C. Ampe: The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins. Biochemistry 38, 3246- 3257 (1999).
141. Kubota, S., H. Kubota & K. Nagata: Cytosolic chaperonin protects folding intermediates of G-beta from aggregation by recognizing hydrophobic beta-strands. Proc Natl Acad Sci U S A 103, 8360-8365 (2006). (Pubitemid 43838460)
142. Spiess, C., E. J. Miller, A. J. McClellan & J. Frydman: Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins. Mol Cell 24, 25-37 (2006). (Pubitemid 44466686)
143. Waldmann, T., E. Nimmesgern, M. Nitsch, J. Peters, G. Pfeifer, S. Müller, J. Kellermann, A. Engel, F. U. Hartl & W. Baumeister: The thermosome of Thermoplasma acidophilum and its relationship to the eukaryotic chaperonin TRiC. Eur J Biochem 227, 848-56 (1995).
144. Yoshida, T., M. Yohda, T. Iida, T. Maruyama, H. Taguchi, K. Yazaki, T. Ohta, M. Odaka, I. Endo & Y. Kagawa: Structural and functional characterization of homo-oligomeric complexes of alpha and beta chaperonin subunits from the hyperthermophilic archaeum Thermococcus strain KS-1. J Mol Biol 273, 635-645 (1997). (Pubitemid 27488805)
145. Reissmann, S., C. Parnot, C. R. Booth, W. Chiu & J. Frydman: Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins. Nat Struct Mol Biol 14, 432-440 (2007). (Pubitemid 46685886)
146. Guagliardi, A., L. Cerchia & M. Rossi: Prevention of in vitro protein thermal aggregation by the Sulfolobus solfataricus chaperonin. Evidence for nonequivalent binding surfaces on the chaperonin molecule. J Biol Chem 270, 28126-28132 (1995).
147. Bosch, G., W. Baumeister & L. O. Essen: Crystal structure of the beta-apical domain of the thermosome reveals structural plasticity in the protrusion region. J Mol Biol 301, 19-25 (2000).
148. Klumpp, M., W. Baumeister, & L. O. Essen: Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin. Cell 91, 263-270 (1997). (Pubitemid 27456393)
149. Gómez-Puertas, P., J. Martín-Benito, J. L. Carrascosa, K. R. Willison & J. M. Valpuesta: The substrate recognition mechanisms in chaperonins. J Mol Recognit 17, 85-94 (2004). (Pubitemid 38370590)
150. Geissler, S., K. Siegers & E. Schiebel: A novel protein complex promoting formation of functional alphaand gamma-tubulin. EMBO J 17, 952-966 (1998). (Pubitemid 28077650)
151. Vainberg, I. E., S. A. Lewis, H. Rommelaere, C. Ampe, J. Vandekerckhove, H. L. Klein & N. J. Cowan: Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin. Cell 93, 863-873 (1998). (Pubitemid 28257591)
152. Hansen, W. J., N. J. Cowan & W. J. Welch: Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins. J Cell Biol 145,, 265-277 (1999). (Pubitemid 29198300)
153. Siegers, K., T. Waldmann, M. R. Leroux, K. Grein, A. Shevchenko, E. Schiebel & F. U. Hartl : Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18, 75-84 (1999). (Pubitemid 29005025)
154. Leroux, M. R., M. Fändrich, D. Klunker, K. Siegers, A. N. Lupas, J. R. Brown, E. Schiebel, C. M. Dobson & F. U. Hartl: MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin. EMBO J 18, 6730-6743 (1999).
155. Whitehead T. A., B. B. Boonyaratanakornkit, V. Höllrigl, & D. S. Clark: A filamentous molecular chaperone of the prefoldin family from the deep-sea hyperthermophile Methanocaldococcus jannaschii. Protein Sci 16, 626-634 (2007). (Pubitemid 46506991)
156. Siegert, R., M. R. Leroux, C. Scheufler, F. U. Hartl & I. Moarefi: Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins. Cell 103, 621-632 (2000).
157. Rommelaere, H., M. De Neve, K. Neirynck, D. Peelaers, D. Waterschoot, M. Goethals, N. Fraeyman, J. Vandekerckhove & C. Ampe: Prefoldin recognition motifs in the nonhomologous proteins of the actin and tubulin families. J Biol Chem 276, 41023-41028 (2001).
158. Martín-Benito, J., J. Boskovic, P. Gómez-Puertas, J. L. Carrascosa, C. T. Simons, S. A. Lewis, F. Bartolini, N. J. Cowan & J. M. Valpuesta: Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT. EMBO J 21, 6377-6386 (2002). (Pubitemid 35448416)
159. Okochi, M., T. Yoshida, T. Maruyama, Y. Kawarabayasi, H. Kikuchi & M. Yohda: Pyrococcus prefoldin stabilizes protein-folding intermediates and transfers them to chaperonins for correct folding. Biochem Biophys Res Commun 291, 769-774 (2002). (Pubitemid 34694341)
160. Simons, C. T., A. Staes, H. Rommelaere, C. Ampe, S. A. Lewis & N. J. Cowan: Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding. J Biol Chem 279, 4196-4203 (2004). (Pubitemid 38199006)
161. Lundin, V. F., P. C. Stirling, J. Gomez-Reino, J. C. Mwenifumbo, J. M. Obst, J. M. Valpuesta & M. R. Leroux: Molecular clamp mechanism of substrate binding by hydrophobic coiled-coil residues of the archaeal chaperone prefoldin. Proc Natl Acad Sci U S A 101, 4367-4372 (2004). (Pubitemid 38437418)
162. Okochi, M., T. Nomura, T. Zako, T. Arakawa, R. Iizuka, H. Ueda, T. Funatsu, M. Leroux & M. Yohda: Kinetics and binding sites for interaction of the prefoldin with a group II chaperonin: contiguous non-native substrate and chaperonin binding sites in the archaeal prefoldin. J Biol Chem 279, 31788-31795 (2004). (Pubitemid 39037851)
163. Zako, T., R. Iizuka, M. Okochi, T. Nomura, T. Ueno, H. Tadakuma, M. Yohda & T. Funatsu: Facilitated release of substrate protein from prefoldin by chaperonin. FEBS Letters 579, 3718-3724 (2005). (Pubitemid 40897715)
164. Zako, T., Y. Murase, R. Iizuka, T. Yoshida, T. Kanzaki, N. Ide, M. Maeda, T. Funatsu & M. Yohda: Localization of prefoldin interaction sites in the hyperthermophilic group II chaperonin and correlations between binding rate and protein transfer rate. J Mol Biol 364, 110-120 (2006). (Pubitemid 44634529)
165. Stirling, P. C., S. F. Bakhoum, A. B. Feigl & M. R. Leroux: Convergent evolution of clamp-like binding sites in diverse chaperones. Nat Struct Mol Biol 13, 865-870 (2006). (Pubitemid 44527367)
166. Kowalski, J. M., R. M. Kelly, J. Konisky, D. S. Clark & K. D. Wittrup: Purification and functional characterization of a chaperone from Methanococcus jannaschii. Syst Appl Microbiol 21, 173-178 (1998). (Pubitemid 28379501)
167. Minuth, T., G. Frey, P. Lindner, R. Rachel, K. O. Stetter & R. Jaenicke: Recombinant homo- and heterooligomers of an ultrastable chaperonin from the archaeon Pyrodictium occultum show chaperone activity in vitro. Eur J Biochem 258, 837-845 (1998). (Pubitemid 28557953)
168. Yoshida, T., R. Kawaguchi, H. Taguchi, M. Yoshida, T. Yasunaga, T. Wakabayashi, M. Yohda & T. Maruyama: Archaeal group II chaperonin mediates protein folding in the cis-cavity without a detachable GroES-like cochaperonin. J Mol Biol 315, 73-85 (2002). (Pubitemid 34722112)