Skip to main content
SpringerLink
Log in

The chaperonin containing t-complex polypeptide 1 (TCP-1)

Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol

  • Chapter
EJB Reviews

Part of the book series: European Journal of Biochemistry ((EJB REVIEWS,volume 1995))

Abstract

Many proteins in the cell require assistance from molecular chaperones at stages in their life cycles in order to attain correctly folded states and functional conformations during protein synthesis or during recovery from denatured states. A recently discovered molecular chaperone, which is abundant in the eukaryotic cytosol and is called the chaperonin containing TCP-1 (CCT), has been shown to assist the folding of some proteins in cytosol. This chaperone is a member of the chaperonin family which includes GroEL, 60-kDa heat shock protein (Hsp60), Rubisco subunit binding protein (RBP) and thermophilic factor 55 (TF55), but is distinct from the other members in several respects. Presently the most intriguing feature is the hetero-oligomeric nature of the CCT; at least eight subunit species which are encoded by independent and highly diverged genes are known. These genes are calculated to have diverged around the starting point of the eukaryotic lineage and they are maintained in all eukaryotes investigated, suggesting a specific function for each subunit species. The amino acid sequences of these subunits share approximately 30% identity and have some highly conserved motifs probably responsible for ATPase function, suggesting this function is common to all subunits. Thus, each subunit is thought to have both specific and common functions. These observations, in conjunction with biochemical and genetic analysis, suggest that CCT functions as a very complex machinery for protein folding in the eukaryotic cell and that its chaperone activity may be essential for the folding and assembly of various newly synthesized polypeptides. This complex behaviour of CCT may have evolved to cope with the folding and assembly of certain highly evolved proteins in eukaryotic cells.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
eBook
USD 16.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Abbreviations

CCT:

chaperonin containing TCP-1

Ccta,Cctb,Cctg,Cctd,Ccte,Cctz,Ccth and cctq :

genes encoding α, β, γ, δ, ε, ζ, η and θ subunits of CCT, respectively

Hsp60:

60-kDa heat-shock protein

MHC:

major histocompatibility complex

Rubisco:

ribulose-bisphosphate carboxylase

RBP:

Rubisco subunit binding protein

t-complex:

the gene complex of mouse chromosome 17 producing the tailless phenotype

TCP-1:

t-complex polypeptide 1

TF55:

thermophilic factor 55

TRD:

transmission ratio distortion

References

  • Andersson, L. (1988) Genetic polymorphism of a bovine t-complex gene (TCP1) linkage to major histocompatibility genes, J. Hered. 79, 1–5.

    PubMed  CAS  Google Scholar 

  • Ashworth, A., Malik, A. N., Walkley, N. A., Kubota, H. and Willison, K. R. (1994) The Tcp-l-related gene, Cctg, maps to mouse chromosome 3, Mammal. Genonze 5, 509–510.

    Google Scholar 

  • Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D. C., Joachimiak, A., Horwich, A. L. and Sigler, P. B. (1994) The crystal structure of the bacterial chaperonin GroEL at 2.8 A, Nature 371, 578–586.

    PubMed  CAS  Google Scholar 

  • Chen, S., Roseman, A. M., Hunter, A. S., Wood, S. P., Burston, S. G., Ranson, N. A., Clarks, A. R. and Saibil, H. R. (1994) Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy, Nature 371, 261–264.

    PubMed  CAS  Google Scholar 

  • Chen, X., Sullivan, D. S. and Huffaker, T. C. (1994) Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo, Proc. Natl Acad. Sci. USA 91, 9111–9115.

    Google Scholar 

  • Cheng, M. Y., Hard, F.-U., Martin, J., Pollock, R. A., Kalousek, F., Neupert, W., Hallberg, E. M., Hallberg, R. L. and Horwich, A. L. (1989) Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria, Nature 337, 620–625.

    PubMed  CAS  Google Scholar 

  • Corbett, J. and Dunn, M. J. (1992) Two-dimensional polyacrylamide gel electrophoresis of membrane proteins, in Methods in molecular biology (Graham, J. M. and Higgins, J. A., eds) vol. 19, pp. 219–227

    Google Scholar 

  • Creutz, C. E., Liou, A., Snyder, S. L., Brownawell, A. and Willison, K. (1994) Identification of the major chromaffin granule-binding protein, chromobindin A, as the cytosolic chaperonin CCT (chaperonin containing TCP-1), J. Biol. Chem. 269, 32035–32038.

    Google Scholar 

  • Dudley, K., Potter, J., Lyon, M. F. and Willison, K. (1984) Analysis of male sterile mutations in the mouse using haploid stage expressed cDNA probes, Nucleic Acids Res. 12, 4281–4293.

    PubMed  CAS  Google Scholar 

  • Ehmann, B., Krenz, M., Mummert, E. and Schafer, E. (1993) Two Tcp-1related but highly divergent gene families exist in oat encoding proteins of assumed chaperone function, FEBS Lett. 336, 313–316.

    PubMed  CAS  Google Scholar 

  • Ellis, R. J. (1990) Molecular chaperones: the plant connection, Science 250, 954–959.

    PubMed  CAS  Google Scholar 

  • Ellis, R. J. (1992) Cytosolic chaperonin confirmed, Nature 358, 191–192.

    PubMed  CAS  Google Scholar 

  • Ellis, R. J. (1994) Chaperoning nascent proteins, Nature 370, 96–97

    PubMed  CAS  Google Scholar 

  • Ellis, R. J. and van der Vies, S. M. (1991) Molecular Chaperones, Annu. Rev. Biochem. 60, 321–347.

    Google Scholar 

  • Fenton, W. A., Kashi, Y., Furtak, K. and Horwich, A. L. (1994) Residues in chaperonin GroEL polypeptide binding and release, Nature 371, 614–619.

    PubMed  CAS  Google Scholar 

  • Frydman, J., Nimmesgem, E., Erdjument-Bromage, H., Wall, J. S., Tempst, P. and Hartl, F.-U. (1992) Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits, EMBO J. 11, 4767–4778.

    PubMed  CAS  Google Scholar 

  • Frydman, J., Nimmesgern, E., Ohtsuka, K. and Hard, F.-U. (1994) Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones, Nature 370, 111–117.

    PubMed  CAS  Google Scholar 

  • Gao, Y., Thomas, J. O., Chow, R. L., Lee, G.-H. and Cowan, N. J. (1992) A cytoplasmic chaperonin that catalyze /3-actin folding, Cell 69, 1043–1050.

    PubMed  CAS  Google Scholar 

  • Gao, Y., Vainberg, I. E., Chow, R. L. and Cowan, N. J. (1993) Two cofactors and cytoplasmic chaperonin are required for the folding of a-and ß-tubulin, Mol. Cell Biol. 13, 2478–2485.

    Google Scholar 

  • Gao, Y, Melki, R., Walden, P. D., Lewis, S. A., Ampe, C., Rommelaere, H., Vandekerckhove, J. and Cowan, N. J. (1994) A novel cochaperonin that modulates the ATPase activity of cytoplasmic chaperonin, J. Cell Biol. 125, 989–996.

    PubMed  CAS  Google Scholar 

  • Georgopoulos, C. P., Hendrix, R. W., Casjens, S. R. and Kaiser, A. D. (1973) Host participation in bacteriophage lambda head assembly, J. Mol. Biol. 76, 45–60.

    Google Scholar 

  • Gething, M.-J. and Sambrook, J. (1992) Protein folding in the cell. Nature 355, 33 —45.

    Google Scholar 

  • Gray, T. E., Eder, J., Bycroft, M., Day, A. G. and Fersht, A. R. (1993) Refolding of barnase mutants and pro-bamase in the presence and absence of GroEL, EMBO J. 12, 4145–4150.

    PubMed  CAS  Google Scholar 

  • Guagliardi, A., Cerchia, L., Bartolucci, S. and Rossi, M. (1994) The chaperonin from archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro, Protein Sci. 3, 1436–1443.

    PubMed  CAS  Google Scholar 

  • Gupta, R. S. (1990) Sequence and structural homology between a mouse t-complex protein TCP-1 and the `chaperonin’ family of bacterial (GroEL, 60–65 kDa heat shock antigen) and eukaryotic proteins, Biochem. Int. 20, 833 —841.

    Google Scholar 

  • Gus-Mayer, S., Brunner, H., Schneider-Poetsch, H. A. W., Lottspeich, E, Eckerskom, C., Grimn, R. and Rudiger, W. (1994) The amino acid sequence previously attributed to a protein kinase or a TCP-1 related molecular chaperone and co-purified with phytochrome is a ß-glucosidase, FEBS Lett. 347, 51–54.

    PubMed  CAS  Google Scholar 

  • Harrison-Lavoie, K. J., Lewis, V. A., Hynes, G. M., Collison, K. S., Nutland, E. and Willison, K. R. (1993) A 102 kDa subunit of a Golgi-associated particles has homology to ß subunits of trimeric G proteins, EMBO J. 12, 2847–2853.

    PubMed  CAS  Google Scholar 

  • Hartl, F. U., Martin, J. and Neupert, W. (1992) Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60, Annu. Rev. Biophys. Biomol. Struct. 21, 293–322.

    Google Scholar 

  • Hemmingsen, S. M., Woolford, C., van der Vies, S. M., Tilly, K., Dennis, D. T., Georgopoulos, C. P., Hendrix, R. W. and Ellis, R. J. (1988) Homologous plant and bacterial proteins chaperone oligomeric protein assembly, Nature 333, 330–334.

    PubMed  CAS  Google Scholar 

  • Horwich, A. L., Low, K. B., Fenton, W. A., Hirshfield, I. N. and Furtak, K. (1993) Folding in vivo of bacterial cytoplasmic proteins: role of groEL, Cell 74, 909–917.

    PubMed  CAS  Google Scholar 

  • Horwich, A. L. and Willison, K. R. (1993) Protein folding in the cell: function of two families of molecular chaperone, hsp60 and TF55TCP1, Phil. Trans. R. Soc. Lond. 339, 313–326.

    Google Scholar 

  • Hynes, G., Kubota, H. and Willison, K. R. (1995) Antibody characterisation of two distinct conformations of the chaperonin containing TCP-1 from mouse testis, FEBS Lett. 358, 129–132.

    PubMed  CAS  Google Scholar 

  • Joly, E. C., Sevigny, G., Todorov, I. T. and Bibor-Hardy, V. (1994a) cDNA encoding a novel TCP-1-related protein, Biochim. Biophys. Acta 1217, 224–226.

    Google Scholar 

  • Joly, E. C., Tremblay, E., Tanguay, R. M., Wu, Y. and Bibor-Hardy, V. (1994b) TRiC-P5, a novel TCP-1-related protein is located in the cytoplasm and in the nuclear matrix, J. Cell Sci. 107, 2851–2859.

    PubMed  CAS  Google Scholar 

  • Khan, A. S., Wilcox, A. S., Polymeropoulos, M. H., Hopkins, J. A., Stevens, T. J., Robinson, M., Orpana, A. K. and Sikela, J. M. (1992) Single pass sequencing and physical and genetic mapping of human brain cDNAs, Nature Genetics 2, 180–185.

    PubMed  CAS  Google Scholar 

  • Kim, S., Willison, K. R. and Horwich, A. L. (1994) Cytosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains, Trends Biochem. Sci. 19, 543–548.

    Google Scholar 

  • Kimura, M. (1983) in The neutral theory of molecular evolution, Cambridge University Press, Cambridge.

    Google Scholar 

  • Kirchhoff, C. and Willison, K. R. (1990) Nucleotide and amino-acid sequence of human testis-derived TCP1, Nucleic Acids Res. 18, 4247.

    PubMed  CAS  Google Scholar 

  • Knapp, S., Schmidt-Krey, I., Hebert, H., Bergman, T., Jomvall, H. and Ladenstein, R. (1994) The molecular chaperonin TF55 from archaeon Sulfolobus solfataricus,.1. Mol. Biol. 242, 397–407.

    Google Scholar 

  • Kolb, V. A., Makeyev, E. V. and Spirit’, A. S. (1994) Folding of firefly luciferase during translation in a cell-free system, EMBO J. 13, 3631–3637.

    PubMed  CAS  Google Scholar 

  • Koll, H., Guiard, B., Rassow, J., Osterman, J., Horwich, A. L., Neupert, W. and Hartl, F.-U. (1992) Antifolding activity of hsp 60 couples protein import into the mitochondrial matrix with export to the inter-membrane space, Cell 68, 1163–1175.

    PubMed  CAS  Google Scholar 

  • Kubota, H., Morita, T., Nagata, T., Takemoto, Y, Nozaki, M., Gachelin, G. and Matsushiro, A. (1991) Nucleotide sequence of mouse Tcp-P cDNA, Gene 105, 269–273.

    PubMed  CAS  Google Scholar 

  • Kubota, H., Morita, T., Satta, Y., Nozaki, M. and Matsushiro, A. (1992a) Nucleotide sequence of a mouse Tcp-1 pseudogene: A nucleotide record for a t complex gene carried by an ancestor of the mouse, Mammal. Genome 2, 246–251.

    Google Scholar 

  • Kubota, H., Willison, K., Ashworth, A., Nozaki, M., Miyamoto, H., Yamamoto, H., Matsushiro, A. and Morita, T. (1992b) Structure and expression of the gene encoding t-complex polypeptide 1 (Tcp-1), Gene 120, 207–215.

    PubMed  CAS  Google Scholar 

  • Kubota, H., Hynes, G., Carne, A., Ashworth, A. and Willison, K. (1994) Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin, Curr. Biol. 4, 89–99.

    Google Scholar 

  • Kubota, H., Hynes, G. and Willison, K. (1995) The eighth Cct gene, Cctq, encoding the theta subunit of the cytosolic chaperonin containing TCP-1, Gene, in the press.

    Google Scholar 

  • Kyte, J. and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein, J. Mol. Biol. 157, 105–132.

    Google Scholar 

  • Langer, T., Lu, C., Echols, H., Flanagan, J., Hayer, M. K. and Hartl, EU. (1992a) Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding, Nature 356, 683–689.

    Google Scholar 

  • Langer, T., Pfeifer, G., Martin, J., Baumeister, W. and Hartl, E-U. (1992b) Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accomodates the protein substrate within its central cavity, EMBO J. 11, 4757–4765.

    Google Scholar 

  • Lewis, V. A., Hynes, G. M., Zheng, D., Saibil, H. and Willison, K. (1992) T-complex polypeptide-1 is a subunit öf a heteromeric particle in the eukaryotic cytosol, Nature 358, 249–252.

    PubMed  CAS  Google Scholar 

  • Li, W.-Z., Lin, P., Frydman, J., Boal, T. R., Cardillo, T. S., Richard, L. M., Toth, D., Lichtman, M. A., Hartl, F.-U., Sherman, F. and Segel, G. B. (1994) Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and yeast, J. Biol. Chem. 269, 18 616–18 622.

    Google Scholar 

  • Lingappa, J. R., Martin, R. L., Wong, M. L., Gamen, D., Welch, W. J. and Lingappa, V. R. (1994) A eukaryotic cytosolic chaperonin is associated with a high molecular mass intermediate in the assembly of hepatitis B virus capsid, a multimeric particle, J. Cell Biol. 125, 99111.

    Google Scholar 

  • Maercker, C. and Lipps, H. J. (1994) A macronuclear DNA molecule from the hypotrichous ciliate Stylonychia lemnae encoding a t-complex polypeptide 1-like protein, Gene 141, 147–148.

    PubMed  CAS  Google Scholar 

  • Marco, S., Carrascossa, J. L. and Valpuesta, J. M. (1994) Reversible interaction of ß-actin along the channel of the TCP-1 cytoplasmic chaperonin, Biophys. J. 67, 364–368.

    Google Scholar 

  • Martel, R., Cloney, L. P., Pelcher, L. E. and Hemmingsen, S. M. (1990) Unique composition of plastid chaperonin-60: a and f polypeptide-encoding genes are highly divergent, Gene 94, 181–187.

    PubMed  CAS  Google Scholar 

  • Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A. L. and Hartl, F.-U. (1991) Chaperonin-mediated protein folding at the surface of groEL through a `molten globule’-like intermediate, Nature 352, 36–42.

    PubMed  CAS  Google Scholar 

  • Martin, W. H. and Creutz, C. E. (1987) Chromobindin A• a Ca2+ and ATP regulated chromaffin granule binding protein, J. Biol. Chem. 262, 2803–2810.

    Google Scholar 

  • Martin, W. H., Fromer, E. and Creutz, C. E. (1989) Chromobindin A, a Ca2+ and ATP-dependent chromaffin granule is found in a variety of tissues and in yeast, Biochem. Biophys. Res. Commun. 165, 3742.

    Google Scholar 

  • Martin, W. H. and Creutz, C. E. (1990) Interaction of the complex scretory vesicle binding protein chromobindin A with nucleotides, J. Neurochem. 54, 612–619.

    PubMed  CAS  Google Scholar 

  • Mehra, V., Sweetser, D. and Young, R. A. (1986) Efficient mapping of protein antigenic determinants, Proc. Natl Acad. Sci. USA 83, 7013 —7017.

    Google Scholar 

  • Melki, R. and Cowan, N. J. (1994) Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates, Mol. Cell. Biol. 14, 2895–2904.

    Google Scholar 

  • Melki, R., Vainberg, I. E., Chow, R. L. and Cowan, N. J. (1993) Chaperonin-mediated folding of vertebrate actin-related protein and y-tubulin, J. Cell Biol. 122, 1301–1310.

    PubMed  CAS  Google Scholar 

  • Miklos, G. L. G. and Campbell, H. D. (1992) The evolution of domains and the organizational complexities of metazoans, Curr. Opin. Genet. Develop. 2, 902–906.

    Google Scholar 

  • Miklos, D., Caplan, S., Martens, D., Hynes, G., Pitluk, Z., Brown, C., Barrell, B., Horwich, A. L. and Willison, K. (1994) Primary structure and function of a second essential member of heterooligomeric TCP1 chaperonin complex of yeast, TCP1ß, Proc. Natl Acad. Sci. USA 91, 2743–2747.

    Google Scholar 

  • Mori, M., Murata, K., Kubota, H., Yamamoto, A., Matsushiro, A. and Morita, T. (1992) Cloning of a cDNA encoding the Tcp-1 (t complex polypeptide 1) homologue of Arabidopsis thaliana, Gene 122, 381382.

    Google Scholar 

  • Morimoto, R. I., Tissieres, A. and Georgopoulos, C. (1994) Progress and perspectives on the biology of heat shock proteins and molecular chaperones, in The biology of heat shock proteins and molecular chaperones ( Morimoto, R. I., Tissieres, A. and Georgopoulos, C., eds) pp. 1–30, Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY.

    Google Scholar 

  • Morita, T., Kubota, H., Gachelin, G., Nozaki, M. and Matsushiro, A. (1991) Cloning of cDNA encoding rat TCP-1, Biochim. Biophys. Acta 1129, 96–99.

    Google Scholar 

  • Morita, T., Kubota, H., Murata, K., Nozaki, M., Delarbre, C., Willison, K., Satta, Y., Sakaizumi, M., Takahata, N., Gachelin, G. and Matsushiro, A. (1992) Evolution of the mouse t haplotype: Recent and worldwide introgression to Mus Musculus, Proc. Natl Acad. Sci. USA 89, 6851–6855.

    Google Scholar 

  • Morita, T., Kubota, H., Satta, Y. and Matsushiro, A. (1993) Evolution of the mouse t haplotype, in Mechanism of molecular evolution: Introduction to molecular paelopopulation biology (Takahata, N. and Clark, A. G., eds) pp. 151–158

    Google Scholar 

  • Mudryj, M., Devoto, S. H., Heibert, S. W., Hunter, T., Pines, T. and Nevins, J. R. (1991) Cell cycle regulation of E2F transcription factor involuves an interaction with cyclin A, Cell 65, 1243–1253.

    PubMed  CAS  Google Scholar 

  • Mummert, E., Grimm, R., Speth, V., Eckerskorn, C., Schiltz, E., Gatenby, A. A. and Schafer, E. (1993) A TCP-1-related molecular chaperone from plants refolds phytochrome to its photoreversible form, Nature 363, 644–648.

    PubMed  CAS  Google Scholar 

  • Mummert, E., Grimm, R., Speth, V., Eckerskom, C., Schiltz, E., Gatenby, A. A. and Schafer, E. (1994) Erratum, Nature 372, 709. Musgrove, J. E., Johnson, R. A. and Ellis, R. J. (1987) Dissociation of the ribulosebisphosphate-carboxylase large-subunit binding protein into dissimilar subunits, Eur. J. Biochem. 163, 529–534.

    Google Scholar 

  • Paciucci, R. (1994) Role of 300 kDa complexes as intermediates in tubulin folding and dimerization: characterization of a 25 kDa cytosolic protein involved in the GTP-dependent release of monomeric tubulin, Biochem. J. 301, 105–110.

    Google Scholar 

  • Peters, J.-M. (1994) Proteasomes: protein degradation machines of the cell, Trends Biochem. Sci. 19, 377–382.

    Google Scholar 

  • Phipps, B. M., Hoffmann, A., Stetter, K. O. and Baumeister, W. (1991) A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archebacteria, EMBO J. 10, 1711–1722.

    PubMed  CAS  Google Scholar 

  • Phipps, B. M., Typke, D., Hegerl, R., Volker, S., Hoffmann, A., Stetter, K. O. and Baumeister, W. (1993) Structure of a molecular chaperone from a thermophilic archaebacterium, Nature 361, 475–477.

    CAS  Google Scholar 

  • Reading, D. S., Hallberg, R. L. and Myers, A. M. (1989) Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor, Nature 337, 655–659.

    PubMed  CAS  Google Scholar 

  • Rommelaere, H., van Troys, M., Gao, Y., Melki, R., Cowan, N. J., Vandekerckhove, J. and Ampe, C. (1993) Eukaryotic cytosolic chaperonin contains t-complex polypeptide 1 and seven related subunits, Proc. Natl Acad. Sci. USA 90, 11975–11979.

    Google Scholar 

  • Roobol, A. and Carden, M. J. (1993) Identification of chaperonin particles in mammalian brain cytosol and t-complex polypeptide 1 as one of their components, J. Neurochem. 60, 2327–2330.

    PubMed  CAS  Google Scholar 

  • Roobol, A., Holmes, F. E., Hayes, N. V. L., Baines, A. J. and Carden, A. J. (1995) Cytoplasmic chaperonin complex enter neuntes developing in vitro and differ in subunit composition within single cells, J. Cell Sci., in the press.

    Google Scholar 

  • Saffer, J. D., Jackson, S. P. and Annarella, M. B. (1991) Developmental expression of Sp1 in the mouse, Mol. Cell. Biol. 11, 2189–2199.

    Google Scholar 

  • Saibil, H. R., Zheng, D., Roseman, A. M., Hunter, A. S., Watson, G. M. F., Chen, S., auf der Mauer, A., O’Hara, B. P., Wood, S. P., Mann, N. H., Barnett, L. K. and Ellis, R. J. (1993) ATP induces large quaternary rearrangements in a cage-like chaperonin structure, Curr. Biol. 3, 265–273.

    Google Scholar 

  • Saitou, N. and Nei, M. (1987) Neighbor joining method: A new method for reconstructing phylogenetic trees, Mol. Biol. Evol. 4, 406–425. Sanchez, E. R. and Erickson, R. P. (1985) Expression of the Tcp-1 locus of the mouse during early embryogenesis, J. Embryol. Exp. Morph. 89, 113–122.

    Google Scholar 

  • Sanders, B. M., Nguyen, J., Douglass, T. G. and Miller, S. (1994) Heat-inducible proteins that react with antibodies to chaperonin 60 are localized in the nucleus of a fish cell line, Biochem. J. 297, 2125.

    Google Scholar 

  • Segel, G. B., Boal, T. R., Cardillo, T. S., Murant, F. G., Lichtman, M. A. and Sherman, F. (1992) Isolation of a gene encoding a chaperoninlike protein by complementation of yeast amino acid transport mutants with human cDNA, Proc. Natl Acad. Sci. USA 89, 6060–6064.

    Google Scholar 

  • Sevigny, G., Joly, E. C., Bibor-Hardy, V. and Lemieux, N. (1994) Assignment of the human homologue of the mTRiC-P5 gene (TRIC5) to band 1q23 by fluorescence in situ hybridization, Genomics 22, 634–636.

    PubMed  CAS  Google Scholar 

  • Silver, L. M. (1985) Mouse t haplotypes, Annu. Rev. Genet. 19, 179–208.

    Google Scholar 

  • Silver, L. M., Artzt, K. and Bennett, D. (1979) A major testicular cell protein specified by a mouse Tit complex gene, Cell 17, 275–284.

    PubMed  CAS  Google Scholar 

  • Silver, L. M., Kleen, K. C., Distel, R. J. and Hecht, N. B. (1987) Synthesis of mouse t complex proteins during haploid stages of spermatogenesis, Dey. Biol. 119, 605–608.

    Google Scholar 

  • Silver, L. M. and Remis, D. (1987) Five genetically defined regions of mouse t haplotypes are involved in transmission ratio distortion, Genet. Res. Camb. 49, 51–56.

    Google Scholar 

  • Silver, P. A. and Way, J. C. (1993) Eukaryotic DnaJ homologs and the specificity of Hsp70 activity, Cell 74, 5–6.

    PubMed  CAS  Google Scholar 

  • Soares, H., Penque, D., Mouta, C. and Rodrigues-Pousada, C. (1994) A Tetrahymena orthologue of the mouse chaperonin subunit CCTy and its co-expression with tubulin during cilia recovery, J. Biol. Cheni. 269, 29 299–29 307.

    Google Scholar 

  • Sternlicht, H., Fan, G. W., Sternlicht, M. L., Driscoll, J. K., Willison

    Google Scholar 

  • K. and Yaffe, M. B. (1993) The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo, Proc. Natl Acad. Sci. USA 90, 9422–9426.

    Google Scholar 

  • Sun, H. B., Neff, A. W., Mescher, A. L. and Malacinski, G. M. (1995) Expression of the axolotl homologue of mouse chaperonin t-complex protein 1 during early development, Biochim. Biophys. Acta 1260, 157–166.

    Google Scholar 

  • Trent, J. D., Osipiuk, J. and Pinkau, T. (1990) Acquired thermotolerance and heat shock in the extremely thermophilic archaebacterium Sulfolobus spl. strain B12, J. Bacteriol. 172, 1478–1484.

    PubMed  CAS  Google Scholar 

  • Trent, J. D., Nimmesgem, E., Wall, J. S., Hard, E-U. and Horwich, A. L. (1991) A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1, Nature 354, 490–493.

    PubMed  CAS  Google Scholar 

  • Ursic, D. and Culbertson, M. R. (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes, Mol. Cell. Biol. 11, 2629–2640.

    Google Scholar 

  • Ursic, D. and Ganetzky, B. (1988) A Drosophila melanogaster gene encodes a protein homologous to the mouse t complex polypeptide 1, Gene 68, 267–274.

    PubMed  CAS  Google Scholar 

  • Ursic, D., Sedbrook, J. C., Himmel, K. L. and Culbertson, M. R. (1994) The essential yeast Tcpl affects actin and microtubules, Mol. Biol. Cell. 5, 1650–1080.

    Google Scholar 

  • Venner, T. J. and Gupta, R. S. (1990) Nucleotide sequence of mouse HSP60 (chaperonin, GroEL homolog) cDNA, Biochim. Biophys. Acta 1087, 1990.

    Google Scholar 

  • Viitanen, P. V., Gatenby, A. A. and Lorimer, G. H. (1992) Purified chaperonin ( GroEL) interacts with the nonnative states of a multitude of Escherichia coli proteins, Protein Sci. 1, 363–369.

    Google Scholar 

  • Vinh, D. B.-N. and Drubin, D. G. (1994) A yeast TCP-1 like protein is required for actin function in vivo, Proc. Natl Acad. Sci. USA 91, 9116–9120.

    Google Scholar 

  • Warterston, R., Martin, C., Craxton, M., Coulson, A., Hillier, L., Durbin, R., Green, P., Shownkeen, R., Halloran, N., Metzstein, M., Hawkins, T., Wilson, R., Berks, M., Du, Z., Tomas, K., Thierry-Meig, J. and Sulston, J. (1992) A survey of expressed genes in Caenorhabditis elegans, Nature Genetics 1, 114–123.

    Google Scholar 

  • Weissman, J. S., Kashi, Y., Fenton, W. A. and Horwich, A. L. (1994) GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms, Cell 78, 693 —702.

    Google Scholar 

  • Willison, K. R., Dudley, K. and Potter, J. (1986) Molecular cloning and sequence analysis of a haploid expressed gene encoding t complex polypeptide 1, Cell 44, 727–738.

    PubMed  CAS  Google Scholar 

  • Willison, K., Kelly, A., Dudley, K., Goodfellow, P., Spun, N., Groves, V., Gorman, P., Sheer, D. and Trowsdale, J. (1987) The human homologue of the mouse t complex gene, TCP1 is located on chromosome 6 but but not near the ILA region, EMBO J. 6, 1867–1974.

    Google Scholar 

  • Willison, K., Lewis, V., Zuckerman, K. S., Cordell, J., Dean, C., Miller, K., Lyon, M. F. and Marsh, M. (1989) The t complex polypeptide 1 (TCP-1) is associated with the cytoplasmic aspect of Golgi membranes, Cell 57, 621— 632.

    Google Scholar 

  • Willison, K. R., Hynes, G., Davies, P., Goldsborough, A. and Lewis, V. A. (1990) Expression of three t-complex genes, Tcp-1, D17Leh117c3 and D17Leh66, in purified murine spermatogenic cell populations, Gen. Res. Camb. 56, 193–201.

    Google Scholar 

  • Willison, K. R. and Kubota, H. (1994) The structure, function, and Genetics of the chaperonin containing TCP-1 (CCT) in eukaryotic cytosol, in The biology of heat shock proteins and molecular chaperones (Morimoto, R. I., Tissieres, A. and Georgopoulos, C., eds) pp. 299–312, Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY.

    Google Scholar 

  • Xie, X. and Palacios, R. (1994) Cloning and expression of a new mammalian chaperonin gene from a multipotent hematopoietic progenitor clone, Blood 84, 2171–2174.

    PubMed  CAS  Google Scholar 

  • Yaffe, M. B., Fan, G. W., Miklos, D., Horwich, A. L., Stemlicht, M. L. and Stemlicht, H. (1992) TCP1 complex is a molecular chaperone in tubulin biogenesis, Nature 358, 245–248.

    PubMed  CAS  Google Scholar 

  • Yasue, M., Serikawa, T., Kuramoto, T., Mori, M., Higashiguchi, T., Ishizaki, K. and Yamada, J. (1992) Chromosomal assignments of 17 structural genes and 11 related DNA fragments in rats ( Rattus norvegicus) by Southern blot analysis of rat x mouse somatic cell hybrid clones, Genomics 12, 659–664.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institute of Cancer Research, Chester Beatty Laboratories, Cancer Research Campaign Centre for Cell and Molecular Biology, London, England

    Hiroshi Kubota, Gillian Hynes & Keith Willison

  2. Chester Beatty Laboratories, Institute of Cancer Research, 237 Fulham Road, London, England, SW3 6JB

    Keith Willison

Authors
  1. Hiroshi Kubota
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Gillian Hynes
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Keith Willison
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

Copyright information

© 1995 FEBS

About this chapter

Cite this chapter

Kubota, H., Hynes, G., Willison, K. (1995). The chaperonin containing t-complex polypeptide 1 (TCP-1). In: EJB Reviews. European Journal of Biochemistry, vol 1995. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-85252-7_11

Download citation

  • DOI: https://doi.org/10.1007/978-3-642-85252-7_11

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-60984-1

  • Online ISBN: 978-3-642-85252-7

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation