Biology:TRiC (complex)

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Short description: Multiprotein complex used in cellular proteostasis
Structure of Saccharomyces cerevisiae TRiC in the AMP-PNP bound state (PDB 5GW5).[1]

T-complex protein Ring Complex (TRiC), otherwise known as Chaperonin Containing TCP-1 (CCT),[lower-alpha 1] is a multiprotein complex and the chaperonin of eukaryotic cells. Like the bacterial GroEL, the TRiC complex aids in the folding of ~10% of the proteome, and actin and tubulin are some of its best known substrates.[2][3] TRiC is an example of a biological machine that folds substrates within the central cavity of its barrel-like assembly using the energy from ATP hydrolysis.

Subunits

The human TRiC complex is formed by two rings containing 8 similar but non-identical subunits, each with molecular weights of ~60 kDa. The two rings are stacked in an asymmetrical fashion, forming a barrel-like structure with a molecular weight of ~1 MDa.[2][3]

Subunit MW (kDa)[A] Features
TCP1 (CCT1/α) 60
CCT2 (β) 57
CCT3 (γ) 61
CCT4 (δ) 58
CCT5 (ε) 60
CCT6 (ζ) 58 Two copies in human genome, CCT6A and CCT6B.
CCT7 (η) 59
CCT8 (θ) 60

A Molecular weight of human subunits.

Counterclockwise from the exterior, each ring is made of the subunits in the following order: 6-8-7-5-2-4-1-3.[4]

Evolution

The CCT evolved from the archaeal thermosome ~2Gya, with the two subunits diversifying into multiple units. The CCT changed from having one type of subunit, to having two, three, five, and finally eight types.[4](fig. 4)

See also

Notes

  1. ↑ The term "TCP-1" is variously expanded as "T-complex protein 1" and "tailless complex polypeptide 1". The "T-complex" is the same as tailless complex, a CCT locus associated with tail length in mice.

References

  1. ↑ Zang, Yunxiang; Jin, Mingliang; Wang, Huping; Cui, Zhicheng; Kong, Liangliang; Liu, Caixuan; Cong, Yao (2016-10-24). "Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM". Nature Structural & Molecular Biology (Springer Science and Business Media LLC) 23 (12): 1083–1091. doi:10.1038/nsmb.3309. ISSN 1545-9993. PMID 27775711. 
  2. ↑ 2.0 2.1 Balchin, David; Hayer-Hartl, Manajit; Hartl, F. Ulrich (2016-06-30). "In vivo aspects of protein folding and quality control". Science (American Association for the Advancement of Science (AAAS)) 353 (6294): aac4354. doi:10.1126/science.aac4354. ISSN 0036-8075. PMID 27365453. 
  3. ↑ 3.0 3.1 Gestaut, Daniel; Limatola, Antonio; Joachimiak, Lukasz; Frydman, Judith (2019). "The ATP-powered gymnastics of TRiC/CCT: an asymmetric protein folding machine with a symmetric origin story". Current Opinion in Structural Biology (Elsevier BV) 55: 50–58. doi:10.1016/j.sbi.2019.03.002. ISSN 0959-440X. PMID 30978594. 
  4. ↑ 4.0 4.1 Willison, KR (5 October 2018). "The structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring.". The Biochemical Journal 475 (19): 3009–3034. doi:10.1042/BCJ20170378. PMID 30291170. 



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