F
IPR012718

T-complex protein 1, epsilon subunit

InterPro entry
Short nameChap_CCT_epsi
Overlapping
homologous
superfamilies
 
family relationships

Description

Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC
[13, 5]
. Chaperonins are involved in productive folding of proteins
[1]
. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal equivalent group II chaperonin is often called the thermosome
[12]
. Both the thermosome and the TCP-1 family of proteins are weakly, but significantly
[14]
, related to the cpn60/groEL chaperonin family (see
IPR001844
).

The TCP-1 protein was first identified in mice where it is especially abundant in testis but present in all cell types. It has since been found and characterised in many other animal species, as well as in yeast, plants and protists. The TCP1 complex has a double-ring structure with central cavities where protein folding takes place
[9]
. TCP-1 is a highly conserved protein of about 60kDa (556 to 560 residues) which participates in a hetero-oligomeric 900kDa double-torus shaped particle
[4]
with 6 to 8 other different, but homologous, subunits
[6]
. These subunits, the chaperonin containing TCP-1 (CCT) subunit beta, gamma, delta, epsilon, zeta and eta are evolutionary related to TCP-1 itself
[15, 3]
. Non-native proteins are sequestered inside the central cavity and folding is promoted by using energy derived from ATP hydrolysis
[2, 7, 8]
. The CCT is known to act as a molecular chaperone for tubulin, actin and probably some other proteins
[10, 11]
.

This family consists exclusively of the CCT epsilon chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.

References

1.Chaperonin-mediated protein folding. Thirumalai D, Lorimer GH. Annu Rev Biophys Biomol Struct 30, 245-69, (2001). View articlePMID: 11340060

2.Protein folding: versatility of the cytosolic chaperonin TRiC/CCT. Leroux MR, Hartl FU. Curr. Biol. 10, R260-4, (2000). View articlePMID: 10753735

3.Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains. Kim S, Willison KR, Horwich AL. Trends Biochem. Sci. 19, 543-8, (1994). View articlePMID: 7846767

4.T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol. Lewis VA, Hynes GM, Zheng D, Saibil H, Willison K. Nature 358, 249-52, (1992). View articlePMID: 1630492

5.TCP1 - molecular chaperonin of the cytoplasm? Nelson RJ, Craig EA. Curr. Biol. 2, 487-9, (1992). View articlePMID: 15335898

6.The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol. Kubota H, Hynes G, Willison K. Eur. J. Biochem. 230, 3-16, (1995). View articlePMID: 7601114

7.Group II chaperonins: new TRiC(k)s and turns of a protein folding machine. Gutsche I, Essen LO, Baumeister W. J. Mol. Biol. 293, 295-312, (1999). View articlePMID: 10550210

8.Structure and function of a protein folding machine: the eukaryotic cytosolic chaperonin CCT. Valpuesta JM, Martin-Benito J, Gomez-Puertas P, Carrascosa JL, Willison KR. FEBS Lett. 529, 11-6, (2002). View articlePMID: 12354605

9.4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement. Cong Y, Baker ML, Jakana J, Woolford D, Miller EJ, Reissmann S, Kumar RN, Redding-Johanson AM, Batth TS, Mukhopadhyay A, Ludtke SJ, Frydman J, Chiu W. Proc. Natl. Acad. Sci. U.S.A. 107, 4967-72, (2010). View articlePMID: 20194787

10.Activities of the chaperonin containing TCP-1 (CCT): implications for cell cycle progression and cytoskeletal organisation. Brackley KI, Grantham J. Cell Stress Chaperones 14, 23-31, (2009). View articlePMID: 18595008

11.The substrate recognition mechanisms in chaperonins. Gomez-Puertas P, Martin-Benito J, Carrascosa JL, Willison KR, Valpuesta JM. J. Mol. Recognit. 17, 85-94, (2004). View articlePMID: 15027029

12.Review: nucleotide binding to the thermoplasma thermosome: implications for the functional cycle of group II chaperonins. Steinbacher S, Ditzel L. J. Struct. Biol. 135, 147-56, (2001). View articlePMID: 11580264

13.Protein folding. Cytosolic chaperonin confirmed. Ellis J. Nature 358, 191, (1992). View articlePMID: 1352857

14.What is a chaperonin? Hemmingsen SM. Nature 357, 650, (1992). View articlePMID: 1352040

15.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. 4, 89-99, (1994). View articlePMID: 7953530

GO terms

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