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Gene Review

Gm12141  -  predicted gene 12141

Mus musculus

Synonyms: Hspd1, Hspd1-1p, OTTMUSG00000005441, chaperonin
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Disease relevance of Hspd1


High impact information on Hspd1

  • The chaperonin GroEL is able to mediate protein folding in its central cavity [6].
  • Folding of the major cytoskeletal components in the cytosol of mammalian cells is mediated by interactions with t-complex polypeptide-1 (TCP1) molecular chaperones, a situation analogous to the chaperonin 60-aided folding of polypeptides in bacteria, chloroplasts and mitochondria [7].
  • Here we report for the first time that a protein, identified by a monoclonal antibody to be the Mt heat shock protein (Baird, P.N., L.M. Hall, and A.R.M. Coates. 1989. J. Gen. Microbiol. 135:931-939) chaperonin (cpn) 10, is responsible for the osteolytic activity of this bacterium [1].
  • Here we find that upon ATP binding, mimicked by the non-hydrolysable analog AMP-PNP (5'-adenylyl-imido-diphosphate), to both CCT-alpha-actin and CCT- beta-tubulin complexes, the chaperonin component undergoes concerted movements of the apical domains, resulting in the cavity being closed off by the helical protrusions of the eight apical domains [8].
  • Structure of a trimeric domain of the MHC class II-associated chaperonin and targeting protein Ii [9].

Biological context of Hspd1


Anatomical context of Hspd1


Associations of Hspd1 with chemical compounds


Physical interactions of Hspd1

  • Analysis of the nascent translation products for folding intermediates has identified a major intermediate that contains all three myosin subunits in a complex with the eukaryotic cytosolic chaperonin [23].
  • The receptor-associated protein, RAP, is a chaperonin-like molecule that binds to two members of the low density lipoprotein receptor (LDLR) superfamily-megalin (gp330) and the LDL receptor-related protein (LRP) [24].

Other interactions of Hspd1


Analytical, diagnostic and therapeutic context of Hspd1

  • Sequence analysis of four candidate genes in this interval revealed a 1349G>A mutation in the chaperonin (delta) subunit 4 (Cct4) gene associated with the mf mutant [27].
  • In analogy to GroEL, changes in shape of the cytosolic chaperonin have been detected in the presence of MgATP using electron microscopy but, in contrast to the nucleotide-induced conformational changes in GroEL, no details are available about the specific nature of these changes [28].
  • The three-dimensional reconstruction of apo-CCT-alpha-actin by cryoelectron microscopy shows that actin binds either the CCTbeta-CCTdelta or the CCTepsilon-CCTdelta subunit pairs of the chaperonin in an open and apparently quasi-native conformation [29].
  • Investigations with the latter confirmed that chaperonin 10 is the moiety in pregnancy serum which initiates response in the EPF bioassay [30].
  • Molecular cloning and characterization of a group II chaperonin delta-subunit from soybean [31].


  1. Mycobacterium tuberculosis chaperonin 10 stimulates bone resorption: a potential contributory factor in Pott's disease. Meghji, S., White, P.A., Nair, S.P., Reddi, K., Heron, K., Henderson, B., Zaliani, A., Fossati, G., Mascagni, P., Hunt, J.F., Roberts, M.M., Coates, A.R. J. Exp. Med. (1997) [Pubmed]
  2. Simultaneous overexpression of two stress proteins in rat cardiomyocytes and myogenic cells confers protection against ischemia-induced injury. Lau, S., Patnaik, N., Sayen, M.R., Mestril, R. Circulation (1997) [Pubmed]
  3. Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin. Kubota, H., Hynes, G., Carne, A., Ashworth, A., Willison, K. Curr. Biol. (1994) [Pubmed]
  4. 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? Fossati, G., Izzo, G., Rizzi, E., Gancia, E., Modena, D., Moras, M.L., Niccolai, N., Giannozzi, E., Spiga, O., Bono, L., Marone, P., Leone, E., Mangili, F., Harding, S., Errington, N., Walters, C., Henderson, B., Roberts, M.M., Coates, A.R., Casetta, B., Mascagni, P. J. Bacteriol. (2003) [Pubmed]
  5. Human chaperonin 60 (Hsp60) stimulates bone resorption: structure/function relationships. Meghji, S., Lillicrap, M., Maguire, M., Tabona, P., Gaston, J.S., Poole, S., Henderson, B. Bone (2003) [Pubmed]
  6. Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Mayhew, M., da Silva, A.C., Martin, J., Erdjument-Bromage, H., Tempst, P., Hartl, F.U. Nature (1996) [Pubmed]
  7. A TCP1-related molecular chaperone from plants refolds phytochrome to its photoreversible form. Mummert, E., Grimm, R., Speth, V., Eckerskorn, C., Schiltz, E., Gatenby, A.A., Schäfer, E. Nature (1993) [Pubmed]
  8. The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin. Llorca, O., Martín-Benito, J., Grantham, J., Ritco-Vonsovici, M., Willison, K.R., Carrascosa, J.L., Valpuesta, J.M. EMBO J. (2001) [Pubmed]
  9. Structure of a trimeric domain of the MHC class II-associated chaperonin and targeting protein Ii. Jasanoff, A., Wagner, G., Wiley, D.C. EMBO J. (1998) [Pubmed]
  10. 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. Gupta, R.S. Biochem. Int. (1990) [Pubmed]
  11. Protein folding. Cytosolic chaperonin confirmed. Ellis, J. Nature (1992) [Pubmed]
  12. Disassembly of the cytosolic chaperonin in mammalian cell extracts at intracellular levels of K+ and ATP. Roobol, A., Grantham, J., Whitaker, H.C., Carden, M.J. J. Biol. Chem. (1999) [Pubmed]
  13. The cytosolic chaperonin CCT associates to cytoplasmic microtubular structures during mammalian spermiogenesis and to heterochromatin in germline and somatic cells. Souès, S., Kann, M.L., Fouquet, J.P., Melki, R. Exp. Cell Res. (2003) [Pubmed]
  14. Chaperonin-mediated de novo generation of prion protein aggregates. Stöckel, J., Hartl, F.U. J. Mol. Biol. (2001) [Pubmed]
  15. Substantial CCT activity is required for cell cycle progression and cytoskeletal organization in mammalian cells. Grantham, J., Brackley, K.I., Willison, K.R. Exp. Cell Res. (2006) [Pubmed]
  16. 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin. Llorca, O., Smyth, M.G., Carrascosa, J.L., Willison, K.R., Radermacher, M., Steinbacher, S., Valpuesta, J.M. Nat. Struct. Biol. (1999) [Pubmed]
  17. Cloning, expression, and purification of a functional nonacetylated mammalian mitochondrial chaperonin 10. Dickson, R., Larsen, B., Viitanen, P.V., Tormey, M.B., Geske, J., Strange, R., Bemis, L.T. J. Biol. Chem. (1994) [Pubmed]
  18. Selected subunits of the cytosolic chaperonin associate with microtubules assembled in vitro. Roobol, A., Sahyoun, Z.P., Carden, M.J. J. Biol. Chem. (1999) [Pubmed]
  19. Cytoplasmic chaperonin complexes enter neurites developing in vitro and differ in subunit composition within single cells. Roobol, A., Holmes, F.E., Hayes, N.V., Baines, A.J., Carden, M.J. J. Cell. Sci. (1995) [Pubmed]
  20. Invariant chain induces B cell maturation in a process that is independent of its chaperonic activity. Matza, D., Lantner, F., Bogoch, Y., Flaishon, L., Hershkoviz, R., Shachar, I. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  21. Embryonic origin of preimplantation factor (PIF): biological activity and partial characterization. Roussev, R.G., Coulam, C.B., Kaider, B.D., Yarkoni, M., Leavis, P.C., Barnea, E.R. Mol. Hum. Reprod. (1996) [Pubmed]
  22. Proteomic analysis of diet-induced hypercholesterolemic mice. Park, J.Y., Seong, J.K., Paik, Y.K. Proteomics (2004) [Pubmed]
  23. Myosin II folding is mediated by a molecular chaperonin. Srikakulam, R., Winkelmann, D.A. J. Biol. Chem. (1999) [Pubmed]
  24. The expression of megalin (gp330) and LRP diverges during F9 cell differentiation. Czekay, R.P., Orlando, R.A., Woodward, L., Adamson, E.D., Farquhar, M.G. J. Cell. Sci. (1995) [Pubmed]
  25. Chaperonin-mediated folding of vertebrate actin-related protein and gamma-tubulin. Melki, R., Vainberg, I.E., Chow, R.L., Cowan, N.J. J. Cell Biol. (1993) [Pubmed]
  26. A Tetrahymena orthologue of the mouse chaperonin subunit CCT gamma and its coexpression with tubulin during cilia recovery. Soares, H., Penque, D., Mouta, C., Rodrigues-Pousada, C. J. Biol. Chem. (1994) [Pubmed]
  27. Hereditary sensory neuropathy is caused by a mutation in the delta subunit of the cytosolic chaperonin-containing t-complex peptide-1 (Cct4 ) gene. Lee, M.J., Stephenson, D.A., Groves, M.J., Sweeney, M.G., Davis, M.B., An, S.F., Houlden, H., Salih, M.A., Timmerman, V., de Jonghe, P., Auer-Grumbach, M., Di Maria, E., Scaravilli, F., Wood, N.W., Reilly, M.M. Hum. Mol. Genet. (2003) [Pubmed]
  28. MgATP binding to the nucleotide-binding domains of the eukaryotic cytoplasmic chaperonin induces conformational changes in the putative substrate-binding domains. Szpikowska, B.K., Swiderek, K.M., Sherman, M.A., Mas, M.T. Protein Sci. (1998) [Pubmed]
  29. Mutational screen identifies critical amino acid residues of beta-actin mediating interaction between its folding intermediates and eukaryotic cytosolic chaperonin CCT. McCormack, E.A., Rohman, M.J., Willison, K.R. J. Struct. Biol. (2001) [Pubmed]
  30. The purification of early-pregnancy factor to homogeneity from human platelets and identification as chaperonin 10. Cavanagh, A.C., Morton, H. Eur. J. Biochem. (1994) [Pubmed]
  31. Molecular cloning and characterization of a group II chaperonin delta-subunit from soybean. Nong, V.H., Arahira, M., Phan, V.C., Kim, C.S., Zhang, D., Udaka, K., Fukazawa, C. J. Biochem. (2002) [Pubmed]
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