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Gene Review

TCP1  -  chaperonin-containing T-complex alpha...

Saccharomyces cerevisiae S288c

Synonyms: CCT-alpha, CCT1, T-complex protein 1 subunit alpha, TCP-1-alpha, YD8142.13, ...
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Disease relevance of TCP1

  • Based on the specificity of the Htt-CCT1 interaction, the CCT1 substrate-binding domain may provide a versatile scaffold for therapeutic inhibitors of neurodegenerative disease [1].
  • Conversely, overexpression of a single TRiC subunit, CCT1, is sufficient to remodel Htt-aggregate morphology in vivo and in vitro, and reduces Htt-induced toxicity in neuronal cells [1].

High impact information on TCP1

  • We suggest that TF55 in archaebacteria and TCP1 in the eukaryotic cytosol are members of a new class of molecular chaperones [2].
  • Here we report that ANC2 is an essential gene that encodes a member of the TCP-1 family [3].
  • A yeast TCP-1-like protein is required for actin function in vivo [3].
  • All eight of the CCT1-CCT8 genes encoding the subunits of the Cct chaperonin complex in Saccharomyces cerevisiae have been identified, including three that were uncovered by the systematic sequencing of the yeast genome [4].
  • The deduced amino acid sequence of A550 is 63% identical to the Cc eta subunit of a murine TCP-1-containing chaperonin and more than 35% identical to thermophilic factor 55 from Sulfolobus shibatae, as well as to a number of proteins belonging to the chaperonin TCP-1 family [5].

Biological context of TCP1

  • Cells carrying tcp1 alleles were analyzed after exposure to the appropriate restrictive temperatures by cell viability tests, differential contrast microscopy, fluorescent, and immunofluorescent microscopy of DNA, tubulin, and actin and by determining the DNA content per cell [6].
  • For 29, including the exosome, the chaperonin containing TCP-1, a 3'-messenger RNA degradation complex, and RNA polymerase II, the process suggests atomic details not easily seen by homology, involving the combination of two or more known structures [7].

Anatomical context of TCP1


  1. The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Tam, S., Geller, R., Spiess, C., Frydman, J. Nat. Cell Biol. (2006) [Pubmed]
  2. A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Trent, J.D., Nimmesgern, E., Wall, J.S., Hartl, F.U., Horwich, A.L. Nature (1991) [Pubmed]
  3. A yeast TCP-1-like protein is required for actin function in vivo. Vinh, D.B., Drubin, D.G. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  4. Review: the Cct eukaryotic chaperonin subunits of Saccharomyces cerevisiae and other yeasts. Stoldt, V., Rademacher, F., Kehren, V., Ernst, J.F., Pearce, D.A., Sherman, F. Yeast (1996) [Pubmed]
  5. A 37.5 kb region of yeast chromosome X includes the SME1, MEF2, GSH1 and CSD3 genes, a TCP-1-related gene, an open reading frame similar to the DAL80 gene, and a tRNA(Arg). Rasmussen, S.W. Yeast (1995) [Pubmed]
  6. The essential yeast Tcp1 protein affects actin and microtubules. Ursic, D., Sedbrook, J.C., Himmel, K.L., Culbertson, M.R. Mol. Biol. Cell (1994) [Pubmed]
  7. Structure-based assembly of protein complexes in yeast. Aloy, P., Böttcher, B., Ceulemans, H., Leutwein, C., Mellwig, C., Fischer, S., Gavin, A.C., Bork, P., Superti-Furga, G., Serrano, L., Russell, R.B. Science (2004) [Pubmed]
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