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T-complex protein Ring Complex (TRiC), otherwise known as Chaperonin Containing TCP-1 (CCT), is a
T-complex protein Ring Complex (TRiC), otherwise known as Chaperonin Containing TCP-1 (CCT), is a multiprotein complex
A protein complex or multiprotein complex is a group of two or more associated polypeptide chains. Protein complexes are distinct from multienzyme complexes, in which multiple catalytic domains are found in a single polypeptide chain.
Protein c ...
and the chaperonin
HSP60, also known as chaperonins (Cpn), is a family of heat shock proteins originally sorted by their 60kDa molecular mass. They prevent misfolding of proteins during stressful situations such as high heat, by assisting protein folding. HSP60 bel ...
of eukaryotic cells. Like the bacterial GroEL
GroEL is a protein which belongs to the chaperonin family of molecular chaperones, and is found in many bacteria. It is required for the proper folding of many proteins. To function properly, GroEL requires the lid-like cochaperonin protein comp ...
, the TRiC complex aids in the folding of ~10% of the proteome, and actin
Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils. It is found in essentially all eukaryotic cells, where it may be present at a concentration of over ...
and tubulin
Tubulin in molecular biology can refer either to the tubulin protein superfamily of globular proteins, or one of the member proteins of that superfamily. α- and β-tubulins polymerize into microtubules, a major component of the eukaryotic cytoske ...
are some of its best known substrates. TRiC is an example of a biological machine
A molecular machine, nanite, or nanomachine is a molecular component that produces quasi-mechanical movements (output) in response to specific stimuli (input). In cellular biology, macromolecular machines frequently perform tasks essential for l ...
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. 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.Evolution
The CCT evolved from the archaealthermosome
A thermosome is a group II chaperonin protein complex that functions in archaea. It is the homolog of eukaryotic CCT. This group II chaperonin is an ATP-dependent chaperonin that is responsible for folding or refolding of incipient or denature ...
~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.
See also
* Chaperone *Chaperonin
HSP60, also known as chaperonins (Cpn), is a family of heat shock proteins originally sorted by their 60kDa molecular mass. They prevent misfolding of proteins during stressful situations such as high heat, by assisting protein folding. HSP60 bel ...
*Heat shock protein
Heat shock proteins (HSP) are a family of proteins produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock, but are now known to also be expressed during other stresses including expo ...
Notes
References
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