T-complex 1

From Wikipedia, the free encyclopedia

T-complex 1

Identifiers

TCP1; CCT-alpha; CCT1; CCTa; D6S230E; TCP-1-alpha

External IDs

OMIM: 186980 MGI: 98535 HomoloGene: 5656

Gene ontology
Molecular Function:	• nucleotide binding • ATP binding • unfolded protein binding
Cellular Component:	• pericentriolar material • nuclear heterochromatin • microtubule organizing center • cytosol • chaperonin-containing T-complex
Biological Process:	• protein folding • tubulin folding

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001008897 (mRNA)
NP_001008897 (protein)

NM_013686 (mRNA)
NP_038714 (protein)

Location

Chr 6: 160.12 - 160.13 Mb

Chr 17: 12.76 - 12.77 Mb

Pubmed search

[1]

[2]

T-complex 1, also known as TCP1, is a human gene.^[1]

This gene encodes a molecular chaperone that is member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants of this gene, encoding different isoforms, have been characterized.^[1]

[edit] References

^ ^a ^b Entrez Gene: TCP1 t-complex 1.

[edit] Further reading

Horwich AL, Willison KR (1993). "Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1.". Philos. Trans. R. Soc. Lond., B, Biol. Sci. 339 (1289): 313–25; discussion 325–6. doi:10.1098/rstb.1993.0030. PMID 8098536.
Burston SG, Clarke AR (1997). "Molecular chaperones: physical and mechanistic properties.". Essays Biochem. 29: 125–36. PMID 9189717.
Blanché H, Wright LG, Vergnaud G, et al. (1992). "Genetic mapping of three human homologues of murine t-complex genes localizes TCP10 to 6q27, 15 cM distal to TCP1 and PLG.". Genomics 12 (4): 826–8. PMID 1572657.
Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317–20. PMID 1602151.
Yaffe MB, Farr GW, Miklos D, et al. (1992). "TCP1 complex is a molecular chaperone in tubulin biogenesis.". Nature 358 (6383): 245–8. doi:10.1038/358245a0. PMID 1630491.
Lewis VA, Hynes GM, Zheng D, et al. (1992). "T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol.". Nature 358 (6383): 249–52. doi:10.1038/358249a0. PMID 1630492.
Ursic D, Culbertson MR (1991). "The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes.". Mol. Cell. Biol. 11 (5): 2629–40. PMID 1901944.
Kirchhoff C, Willison K (1990). "Nucleotide and amino-acid sequence of human testis-derived TCP1.". Nucleic Acids Res. 18 (14): 4247. PMID 2377466.
Fonatsch C, Gradl G, Ragoussis J, Ziegler A (1987). "Assignment of the TCP1 locus to the long arm of human chromosome 6 by in situ hybridization.". Cytogenet. Cell Genet. 45 (2): 109–12. PMID 3476253.
Willison K, Kelly A, Dudley K, et al. (1987). "The human homologue of the mouse t-complex gene, TCP1, is located on chromosome 6 but is not near the HLA region.". EMBO J. 6 (7): 1967–74. PMID 3653076.
Roobol A, Holmes FE, Hayes NV, et al. (1995). "Cytoplasmic chaperonin complexes enter neurites developing in vitro and differ in subunit composition within single cells.". J. Cell. Sci. 108 ( Pt 4): 1477–88. PMID 7615668.
Ashworth A (1994). "Two acetyl-CoA acetyltransferase genes located in the t-complex region of mouse chromosome 17 partially overlap the Tcp-1 and Tcp-1x genes.". Genomics 18 (2): 195–8. doi:10.1006/geno.1993.1454. PMID 7904580.
Miklos D, Caplan S, Mertens D, et al. (1994). "Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 beta.". Proc. Natl. Acad. Sci. U.S.A. 91 (7): 2743–7. PMID 7908441.
Chen X, Sullivan DS, Huffaker TC (1994). "Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo.". Proc. Natl. Acad. Sci. U.S.A. 91 (19): 9111–5. PMID 7916460.
Kubota H, Hynes G, Carne A, et al. (1994). "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin.". Curr. Biol. 4 (2): 89–99. PMID 7953530.
Frydman J, Hartl FU (1996). "Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms.". Science 272 (5267): 1497–502. PMID 8633246.
Moudjou M, Bordes N, Paintrand M, Bornens M (1996). "gamma-Tubulin in mammalian cells: the centrosomal and the cytosolic forms.". J. Cell. Sci. 109 ( Pt 4): 875–87. PMID 8718679.
Morrison K, Papapetrou C, Attwood J, et al. (1997). "Genetic mapping of the human homologue (T) of mouse T(Brachyury) and a search for allele association between human T and spina bifida.". Hum. Mol. Genet. 5 (5): 669–74. PMID 8733136.
Masuno M, Fukao T, Song XQ, et al. (1997). "Assignment of the human cytosolic acetoacetyl-coenzyme A thiolase (ACAT2) gene to chromosome 6q25.3-q26.". Genomics 36 (1): 217–8. doi:10.1006/geno.1996.0452. PMID 8812443.