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Gene Review

TCP1  -  T-complex 1

Bos taurus

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High impact information on TCP1

  • The biogenesis of the cytoskeletal proteins actin and tubulin involves interaction of nascent chains of each of the two proteins with the oligomeric protein prefoldin (PFD) and their subsequent transfer to the cytosolic chaperonin CCT (chaperonin containing TCP-1) [1].
  • Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits [2].
  • T-complex polypeptide 1 (TCP-1) was analyzed as a potential chaperonin (GroEL/Hsp60) equivalent of the eukaryotic cytosol [2].
  • We provide evidence that TCP-1 ring complex from bovine testis can facilitate the folding of both actin and tubulin, although, as in the case of chaperonin from reticulocyte lysate, two cofactors are required for the generation of properly folded tubulin [3].
  • Partial amino acid sequence data reveal that one of these is t-complex polypeptide 1 (TCP-1), while the other seven are TCP-1-related polypeptides, implicating the existence of a multigene family of TCP-1 homologues [3].

Biological context of TCP1


Anatomical context of TCP1

  • The chaperonin CCT (chaperonin containing t-complex polypeptide 1 (TCP-1)) from bovine testis was mixed rapidly with different concentrations of ATP and the time-resolved change in fluorescence emission, upon excitation at 280 nm, was followed [6].
  • The results of these studies demonstrate that although the beta gamma T subunit complex increases the association of the alpha T subunit with lipid vesicles that lack the photoreceptor, the beta gamma T complex is not necessary for the binding of alpha T to lipid vesicles containing rhodopsin, provided sufficient amounts of rhodopsin are present [7].

Associations of TCP1 with chemical compounds

  • However, either the dissociation of the activated alpha T subunit from the beta gamma T complex, or a conformational change in beta gamma T which occurs as a result of the subunit dissociation event, appears to be slow relative to the G protein-subunit association event [8].
  • In these cases the alpha T . GTP gamma S inhibitory effects are completely eliminated and the inhibitions observed with holotransducin can be fully accounted for by the beta gamma T complex [9].
  • By using the MIANS moiety as a fluorescent reporter group, we were able to monitor directly the binding of the MIANS-beta gamma T complex to light-activated rhodopsin, which was reconstituted into phosphatidylcholine vesicles, through an enhancement (30-50%) in the MIANS fluorescence [4].
  • Unexpectedly, we find that the dissociation of IAF-beta gamma T from an aluminum fluoride-activated alpha TGDP/IAF-beta gamma T complex occurs prior to the onset of the intrinsic fluorescence changes in alpha T that accompany activation of this subunit [10].
  • Specifically, a beta gamma T complex that was labeled with 5-(iodoacetamido)fluorescein (IAF-beta gamma T) served as a donor for resonance energy transfer and an alpha T-GDP species labeled with eosin 5-isothiocyanate (EITC-alpha TGDP) served as the acceptor [10].

Physical interactions of TCP1

  • These results suggest that this region of the rhodopsin molecule may constitute a portion of the binding domain for the beta gamma T complex [4].

Other interactions of TCP1

  • However, some genes such as Cathepsin B (P = 0.0677), RAD50 (P = 0.0899), and TCP1 (P = 0.0824) tended to show higher expression in the early cleaving than in the late cleaving embryo [11].
  • Conditions which resulted in the activation of the alpha T subunit reversed the alpha T-induced enhancement of the MIANS emission, whereas the rhodopsin-induced enhancement persisted, thereby suggesting that the rhodopsin-beta gamma T complex can remain intact throughout the G protein activation event [4].

Analytical, diagnostic and therapeutic context of TCP1

  • Sequence alignments of peptides generated from both subunits of the thermosome and different subunits of TRiC reveal a high partial similarity to each other and to the archaebacterial chaperonin thermophilic factor 55 from Sulfolobus shibatae as well as to eukaryotic TCP1 proteins [12].


  1. Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT. Martín-Benito, J., Boskovic, J., Gómez-Puertas, P., Carrascosa, J.L., Simons, C.T., Lewis, S.A., Bartolini, F., Cowan, N.J., Valpuesta, J.M. EMBO J. (2002) [Pubmed]
  2. Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. Frydman, J., Nimmesgern, E., Erdjument-Bromage, H., Wall, J.S., Tempst, P., Hartl, F.U. EMBO J. (1992) [Pubmed]
  3. Eukaryotic cytosolic chaperonin contains t-complex polypeptide 1 and seven related subunits. Rommelaere, H., Van Troys, M., Gao, Y., Melki, R., Cowan, N.J., Vandekerckhove, J., Ampe, C. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  4. Rhodopsin/transducin interactions. I. Characterization of the binding of the transducin-beta gamma subunit complex to rhodopsin using fluorescence spectroscopy. Phillips, W.J., Cerione, R.A. J. Biol. Chem. (1992) [Pubmed]
  5. Nested allosteric interactions in the cytoplasmic chaperonin containing TCP-1. Kafri, G., Willison, K.R., Horovitz, A. Protein Sci. (2001) [Pubmed]
  6. Transient kinetic analysis of ATP-induced allosteric transitions in the eukaryotic chaperonin containing TCP-1. Kafri, G., Horovitz, A. J. Mol. Biol. (2003) [Pubmed]
  7. Rhodopsin/transducin interactions. II. Influence of the transducin-beta gamma subunit complex on the coupling of the transducin-alpha subunit to rhodopsin. Phillips, W.J., Wong, S.C., Cerione, R.A. J. Biol. Chem. (1992) [Pubmed]
  8. Labeling of the beta gamma subunit complex of transducin with an environmentally sensitive cysteine reagent. Use of fluorescence spectroscopy to monitor transducin subunit interactions. Phillips, W.J., Cerione, R.A. J. Biol. Chem. (1991) [Pubmed]
  9. Mechanism of guanine nucleotide regulatory protein-mediated inhibition of adenylate cyclase. Studies with isolated subunits of transducin in a reconstituted system. Cerione, R.A., Staniszewski, C., Gierschik, P., Codina, J., Somers, R.L., Birnbaumer, L., Spiegel, A.M., Caron, M.G., Lefkowitz, R.J. J. Biol. Chem. (1986) [Pubmed]
  10. Aluminum fluoride activation of bovine transducin induces two distinct conformational changes in the alpha subunit. Mittal, R., Cerione, R.A., Erickson, J.W. Biochemistry (1994) [Pubmed]
  11. Quantitative expression of candidate genes for developmental competence in bovine two-cell embryos. Dode, M.A., Dufort, I., Massicotte, L., Sirard, M.A. Mol. Reprod. Dev. (2006) [Pubmed]
  12. The thermosome of Thermoplasma acidophilum and its relationship to the eukaryotic chaperonin TRiC. Waldmann, T., Nimmesgern, E., Nitsch, M., Peters, J., Pfeifer, G., Müller, S., Kellermann, J., Engel, A., Hartl, F.U., Baumeister, W. Eur. J. Biochem. (1995) [Pubmed]
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